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dodecamer
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alpha6,beta6, 6 * 47000 + 6 * 51000, SDS-PAGE
heterodecamer
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x * 70000 + x * 60000 + x * 44000 + x * 42000 + x * 36000 + x * 32000 + x * 29000 + x * 16000 + x * 13000 + x * 12000, SDS-PAGE
oligomer
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oligomerization of ATP synthase is critical for the morphology of the inner mitochondrial membrane because it supports the generation of tubular cristae membrane domains, overview. Association of individual F1Fo-ATP synthase complexes is mediated by the membrane-embedded Fo-part. Subunits e, g, k, and i are involved in the stepwise assembly of F1Fo-ATP synthase dimers and oligomers. Subunit i facilitates the incorporation of newly synthesized subunits into ATP synthase complexes, while subunit k stabilizes the dimer. Formation of one dimeric form of ATP synthase is inhibited in the absence of subunit. Detailed overview i
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x * 16000, proteolipid subunit c of V-ATPase, SDS-PAGE
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x * 16000, proteolipid subunit c of V-ATPase, SDS-PAGE
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x * alpha, 52000-53000 + x * beta, 51000 + x * gamma, 40000, SDS-PAGE
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x * 62800, recombinant His3-tagged subunit A of V1VO ATPase, SDS-PAGE
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subunits of F1, x * 54000 + x * 50000 + x * 33000 + x * 17000 + x * 5700, SDS-PAGE
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x * 60000, F1-ATP synthase beta-subunit, SDS-PAGE
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the calculated molecular masses of the deduced gene products are 22.0 kDa (subunit D), 38.7 kDa (subunit C), 11.6 kDa (subunit E), 52.0 kDa (subunit B), and 64.5 kDa (subunit A). The described operon contains genes in the order D, C, E, B, and A. It contains no gene for the hydrophobic, so-called proteolipid (subunit c, the proton-conducting subunit of the A0 part). This subunit is isolated and purified its molecular mass as deduced by SDS-polyacrylamide gel electrophoresis is 9.7 kDa
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x * 70000 (subunit A) + x * 55000 (subunit B), + x * 37000 (subunit C) + x * 12000 (subunit E) + x * 9700 (subunit c), SDS-PAGE
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the calculated molecular masses of the deduced gene products are 22.0 kDa (subunit D), 38.7 kDa (subunit C), 11.6 kDa (subunit E), 52.0 kDa (subunit B), and 64.5 kDa (subunit A). The described operon contains genes in the order D, C, E, B, and A. It contains no gene for the hydrophobic, so-called proteolipid (subunit c, the proton-conducting subunit of the A0 part). This subunit is isolated and purified its molecular mass as deduced by SDS-polyacrylamide gel electrophoresis is 9.7 kDa
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x * 70000 (subunit A) + x * 55000 (subunit B), + x * 37000 (subunit C) + x * 12000 (subunit E) + x * 9700 (subunit c), SDS-PAGE
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x * 68500, catalytic subunit A, calculated from amino acid sequence
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x * 51305, beta subunit, plus x * 14722, epsilon subunit, calculated, plus x * alpha and gamma subunits
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x * 51305, beta subunit, plus x * 14722, epsilon subunit, calculated, plus x * alpha and gamma subunits
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x * 60000, F1-ATP synthase beta-subunit, SDS-PAGE
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x * 100000, subunit a, SDS-PAGE
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x * 100000, subunit a, SDS-PAGE
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x * 59000 + x * 56000 + x * 37000 + x * 17500 + x * 13000, SDS-PAGE
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x * 51526, calculated for beta subunit
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x * 66009, calculated for alpha subunit
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Thermosynechococcus vestitus
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x * 54271, alpha-subunit, mass spectrometry, x * 51795, beta-subunit, mass spectrometry, x * 35013, gamma-subunit, mass sepctrometry, x * 20621, delta-subunit, mass spectrometry, x * 19617, b-subunit, mass spectrometry, x * 15457, b'-subunit, mass spectrometry, x * 14741, epsilon-subunit, mass spectrometry
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x * 40000, subunit ATPaseTb2, SDS-PAGE
dimer
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complex V exhibits an increased stability of its dimeric form
dimer
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complex V exhibits an increased stability of its dimeric form
dimer
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complex V exhibits an increased stability of its dimeric form
multimer
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subunit composition of bacterial F1 and Fo is alpha3beta3gammadeltaepsilon and ab2c10-15, respectively, and the gammaepsilonc10-15 complex rotates against the alpha3beta3deltaab2 complex in FoF1. The epsilon subunit has a molecular mass of 14 kDa and a two-domain structure consisting of an N-terminal 10-stranded beta-sandwich and two C-terminal alpha-helices
multimer
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FOF1-ATP synthase is a multi-subunit protein
multimer
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the ATP synthase enzymes of chloroplasts is composed of two protein segments, FO and F1, the chloroplast FO1 contains four different polypeptide subunits with a stoichiometry of I1II1III14IV1. The F1 segment contains the catalytic sites for ATP synthesis and hydrolysis. The chloroplast F1 is comprised of five different polypeptide subunits, alpha to epsilon, with a stoichiometry of alpha3beta3gamma1delta1epsilon1
nonamer
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alpha3,beta3,tau1,delta1,epsilon1, 3 * 66000 + 3 * 60200 + 1 * 36300 + 1 * 15000 + 1 * 12000, F1 subunit, SDS-PAGE
nonamer
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alpha3,beta3,gamma1,delta1,epsilon1, 1 * 60000 + 3 * 53000 + 1 * 31000 + 1 * 25000 + 1 * 21000, SDS-PAGE
additional information
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x * F1alpha, 55000 + x * F1beta, 50000, + x * F1gamma, 33000, + x * F1delta, 20000, + x * F1epsilon, 18000, SDS-PAGE of strain NASF-1, x * F1alpha, 55000 + x * F1beta, 50000, + x * F1gamma, 30000, + x * F1delta, 23000, + x * F1epsilon, 14000, SDS-PAGE of strain ATCC33020, x * F1alpha, 55500 + x * F1beta, 50500, + x * F1gamma, 33100, + x * F1delta, 19200, + x * F1epsilon, 15100, sequence analysis of strain NASF-1
additional information
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secondary structure analysis by circular dichroism spectroscopy shows that subunit A of V1VO ATPase comprises 43% alpha-helix, 25% beta-sheet and 40% random coil content
additional information
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subunit organisation model, overview
additional information
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subunit organisation model, overview
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additional information
Alkalihalophilus pseudofirmus
subunit organisation model, overview
additional information
Alkalihalophilus pseudofirmus OF4
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subunit organisation model, overview
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additional information
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subunit organisation model, overview
additional information
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subunit organisation model, overview
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additional information
modular assembly of the F1Fo ATP synthase. F1 is an intermediate of assembly of plant F1FO ATP synthase. The catalytic F1 subunit complex alpha3beta3 and FO components subunits (a, c, e, f, g, and A6L (or ATP8)) are connected by a central stalk (including F1 subunits gamma, delta and epsilon) and a peripheral stalk (including OSCP, subunit b, subunit d and F6)
additional information
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subunit organisation model, overview
additional information
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subunit organisation model, overview
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additional information
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subunit organisation model, overview
additional information
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subunit organisation model, overview
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additional information
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subunit organisation model, overview
additional information
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subunit organisation model, overview
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additional information
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subunit organisation model, overview
additional information
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subunit organisation model, overview
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additional information
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subunit organisation model, overview
additional information
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subunit organisation model, overview
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additional information
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four bands alpha, beta, gamma and epsilon in F1 deltasigma with identical molecular mass values as those in the native enzyme, SDS-PAGE
additional information
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structure and location in the ATP synthase of subunit epsilon, sequence comparisons, the subunit epsilon is critically important for binding of F1 to Fo, the epsilon subunit is highly mobile and can interact with residues in subunits alpha, beta, and gamma, overview
additional information
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structure analysis F1 has 2 stable conformational states: ATP-binding dwell state and catalytic dwell state
additional information
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subunit organisation model, overview
additional information
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F1-ATPase is an ATP-driven rotary motor wherein the gamma-subunit rotates against the surrounding alpha3beta3 stator ring. The three catalytic sites of F1-ATPase reside on the interface of the alpha and beta subunits of the alpha3beta3 ring. While the catalytic residues predominantly reside on the beta subunit, the alpha subunit has one catalytically critical arginine, termed the arginine finger
additional information
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F1-ATPase is an ATP-driven rotary motor wherein the gamma-subunit rotates against the surrounding alpha3beta3 stator ring. The three catalytic sites of F1-ATPase reside on the interface of the alpha and beta subunits of the alpha3beta3 ring. While the catalytic residues predominantly reside on the beta subunit, the alpha subunit has one catalytically critical arginine, termed the arginine finger
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additional information
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structure and location in the ATP synthase of subunit epsilon, sequence comparisons, the subunit epsilon is critically important for binding of F1 to Fo, the epsilon subunit is highly mobile and can interact with residues in subunits alpha, beta, and gamma, overview
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additional information
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structure analysis F1 has 2 stable conformational states: ATP-binding dwell state and catalytic dwell state
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additional information
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four bands alpha, beta, gamma and epsilon in F1 deltasigma with identical molecular mass values as those in the native enzyme, SDS-PAGE
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additional information
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subunit organisation model, overview
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additional information
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FoF1-ATPase/synthase consists of two rotary molecular motors: a water-soluble, ATP-driven F1 motor and a membrane embedded, H+-driven Fo motor, F1-ATPase is formed by 5 subunits types: alpha3beta3gammadeltaepsilon. F1-ATPase hydrolysis of one ATP drives discrete 120° rotation of the gammaepsilon subunits relative to the other subunits, structure analysis, overview. Strong inhibitory effect of the TF1 epsilon subunit on nucleotide binding, the presence of the extended epsilon subunit will change the rotational potential profile of gamma and epsilon subunits by changing the free energy difference between the nucleotide binding to high and low affinity binding sites. This may directly relate to the role of the epsilon subunit in efficient ATP synthesis under certain conditions
additional information
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transduction of the conformation signal between catalytic and noncatalytic sites, overview
additional information
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subunit organisation model, overview
additional information
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subunit organisation model, overview
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additional information
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subunit organisation model, overview
additional information
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subunit organisation model, overview
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additional information
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the enzyme is composed of two structurally and functionally distinct sectors, F1 and F0. F1 shows ATPase activity, Fo mediates H+ translocation across the membrane
additional information
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additional information
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additional information
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the whole ATPase, 468000 Da, contains one F1 sector, one oligomycin-sensitivity confering protein, and one chain each of four membrane sector subunits, F1 contains 5 tightly bound subunits
additional information
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subunit composition
additional information
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molecular weight of the subunits, biogenesis of the enzyme depends on a close cooperation of mitochondrial and cytoplasmic synthesis
additional information
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the gamma-subunit of the enzyme complex rotates and turns into the F1 domain, when protons cross the membrane, generating conformation changes in the alpha- and beta-chains, which are responsible for catalysis of ATP synthesis from ADP and phosphate, a reserve gamma-subunit rotation reverses the proton flux and promotes ATP hydrolysis, subunit structure of the F1Fo-ATP synthase complex, overview
additional information
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F1 is a rotary chemical motor and generator, structure modelling, overview
additional information
structure analysis of conformations of the betaE-, betaTP- and betaDP-subunits in ground-state structure of F1-ATPase, catalytic sites and conformational changes, overview
additional information
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structure analysis of conformations of the betaE-, betaTP- and betaDP-subunits in ground-state structure of F1-ATPase, catalytic sites and conformational changes, overview
additional information
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subunit organisation model, overview
additional information
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subunit organisation model, overview
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additional information
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subunit organisation model, overview
additional information
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subunit organisation model, overview
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additional information
Desulforamulus reducens
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subunit organisation model, overview
additional information
Desulforamulus reducens MI-1
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subunit organisation model, overview
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additional information
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size of major subunits
additional information
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x * F1alpha, 55259 + x * F1beta, 50117, + x * F1gamma, 19303, + x * F1epsilon, 14914, + x * F0a, 30275, + x * F0b, 17244, + x * F0c, 8246
additional information
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size of major subunits
additional information
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structure-function relationship of the proton conductor F0
additional information
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F1 is composed of five types of subunits, F0 is composed of three types of subunits, ratio of F1 subunits: alpha3beta3gamma1delta1epsilon1, ratio of F0 subunits: chi2psi2omega10
additional information
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the stoichiometry of subunits in F1 is alpha3beta3gamma1delta1epsilon1, the stoichiometry of F0 subunits is not yet settled
additional information
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subunit composition
additional information
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structure and location in the ATP synthase of subunit epsilon, sequence comparisons, the N-terminal beta-sandwich of the subunit epsilon is critically important for binding of F1 to Fo, the epsilon subunit is highly mobile and can interact with residues in subunits alpha, beta, and gamma, overview
additional information
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homology modeling of the immobilized enzyme, structure, overview
additional information
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F1 is a rotary chemical motor and generator, structure modelling, overview
additional information
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the ATP synthase beta subunit hinge domain dramatically changes in conformation upon nucleotide binding, structure and modelling, overview
additional information
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the epsilon subunit has a molecular mass of 14 kDa and a two-domain structure consisting of an N-terminal 10-stranded beta-sandwich and two C-terminal alpha-helices
additional information
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subunit organisation model, overview
additional information
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subunit organisation model, overview
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additional information
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subunit organisation model, overview
additional information
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subunit organisation model, overview
additional information
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subunit organisation model, overview
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additional information
Halalkalibacterium halodurans
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subunit organisation model, overview
additional information
Halalkalibacterium halodurans C-125
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subunit organisation model, overview
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additional information
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the gamma-subunit of the enzyme complex rotates and turns into the F1 domain, when protons cross the membrane, generating conformation changes in the alpha- and beta-chains, which are responsible for catalysis of ATP synthesis from ADP and phosphate, a reserve gamma-subunit rotation reverses the proton flux and promotes ATP hydrolysis, subunit structure of the F1Fo-ATP synthase complex, overview
additional information
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beta-F1-ATPase is the catalytic subunit of the mitochondrial H+-ATP synthase
additional information
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size of major subunits
additional information
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molecular weight of the subunits, biogenesis of the enzyme depends on a close cooperation of mitochondrial and cytoplasmic synthesis
additional information
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subunit organisation model, overview
additional information
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subunit organisation model, overview
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additional information
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subunit organisation model, overview
additional information
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subunit organisation model, overview
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additional information
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size of major subunits
additional information
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size of major subunits
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additional information
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additional information
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the whole ATPase, 468000 Da, contains one F1 sector, one oligomycin-sensitivity confering protein, and one chain each of four membrane sector subunits, F1 contains 5 tightly bound subunits
additional information
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molecular weight of the subunits, biogenesis of the enzyme depends on a close cooperation of mitochondrial and cytoplasmic synthesis
additional information
three-dimensional structures of wild-type and mutant beta-subunits, overview
additional information
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beta-F1-ATPase is the catalytic subunit of the mitochondrial H+-ATP synthase
additional information
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transduction of the conformation signal between catalytic and noncatalytic sites, linking of catalytic and noncatalytic sites of F1, overview
additional information
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additional information
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additional information
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subunit composition
additional information
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molecular weight of the subunits, biogenesis of the enzyme depends on a close cooperation of mitochondrial and cytoplasmic synthesis
additional information
structure analysis, overview
additional information
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structure analysis, overview
additional information
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subunits alpha, beta, gamma, delta and sigma of the purified chimeric enzyme, with the stoichiometry of 3:3:1:1:1, SDS-PAGE
additional information
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V-ATPase consists of a cytoplasmic domain V1 and a transmembrane domain V0. Both domains contain several subunits. The V0 transmembrane domain consists of subunits a, c, c', c'' and d. Proton translocation takes place at the interface of subunit a and the rotating c, c', and c'' subunits. NMR structure determination, 3D structure of a peptide derived from the putative transmembrane segment 7 of subunit a from H+-V-ATPase determined by solution state NMR in SDS solution. A stable helix is formed from L736 up to and including Q745, the lumenal half of the putative TM7. The helical region extends well beyond A738. The secondary structure of the peptide depends on the pH and the type of detergent used, overview
additional information
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the enzyme is found in monomeric, dimeric and higher oligomeric forms in the inner mitochondrial membrane. Dimerization of ATP synthase complexes is a prerequisite for the generation of larger oligomers that promote membrane bending and formation of tubular cristae membranes. Two small proteins of the membrane-embedded Fo-domain subunits e and g are dimer-specific subunits of yeast ATP synthase and are required for stabilization of the dimers. Subunits e and g sequentially assemble with monomeric ATP synthase to form a dimerization-competent primed monomer, overview
additional information
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beta-F1-ATPase is the catalytic subunit of the mitochondrial H+-ATP synthase
additional information
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subunits alpha, beta, gamma, delta and sigma of the purified chimeric enzyme, with the stoichiometry of 3:3:1:1:1, SDS-PAGE
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additional information
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subunit composition
additional information
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molecular weight of the subunits, biogenesis of the enzyme depends on a close cooperation of mitochondrial and cytoplasmic synthesis
additional information
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in chlorpoplast ATP synthase, both the N-terminus and C-terminus of the epsilon subunit show importance in regulation of the ATPase activity. The N-terminus of the epsilon subunit is more important for its interaction with gamma and some CF0 subunits, and crucial for the blocking of the proton leakage
additional information
structure of the c14 rotor ring of the proton translocating chloroplast ATP synthase, overview
additional information
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structure of the c14 rotor ring of the proton translocating chloroplast ATP synthase, overview
additional information
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comparison of amino acid sequence with alpha subunit and with alpha and beta subunits of Escherichia coli F1-ATPase
additional information
comparison of amino acid sequence with alpha and beta subunits of Escherichia coli Fl-ATPase. Protein shows cross-reactivity with yeast vacuolar H+-ATPase
additional information
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interaction between delta and epsilon subunits
additional information
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the tryptophan residue, located within the N-terminal region of the epsilon subunit is involved in deltaepsilon interaction
additional information
Thermosynechococcus vestitus
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structure-function relationship of the intrinsic inhibitor subunit epsilon subunit in F1 from photosynthetic organism, NMR structure of the epsilon subunits, wild-type and mrecombinant/chimeric, overview. Analysis of the flexibility of the C-terminal domains using molecular dynamics simulations, overview
additional information
9 subunits as calculated from DNA sequence
additional information
9 subunits as calculated from DNA sequence
additional information
9 subunits as calculated from DNA sequence
additional information
9 subunits as calculated from DNA sequence
additional information
9 subunits as calculated from DNA sequence
additional information
9 subunits as calculated from DNA sequence
additional information
9 subunits as calculated from DNA sequence
additional information
9 subunits as calculated from DNA sequence
additional information
9 subunits as calculated from DNA sequence
additional information
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9 subunits as calculated from DNA sequence
additional information
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9 subunits as calculated from DNA sequence
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