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homotetramer
4 * 72397, PDIL2-3, calculated from amino acid sequence
multimer
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x * 52000 + x * ?, SDS-PAGE
oligomer
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x * 62000, gel filtration, x * 56000, calculated
?
x * 55000, SDS-PAGE
?
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x * 56400, calculated from amino acid sequence
?
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x * 75000-80000, SDS-PAGE
?
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x * 47400, calculated from amino acid sequence
?
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x * 54300, calculation from nucleotide sequence
?
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x * 27300, calculated from amino acid sequence
?
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x * 30000, His6-tagged enzyme, SDS-PAGE
?
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x * 25910, calculation from nucleotide sequence
?
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x * 55000, SDS-PAGE, another band with MW 45000 represents a proteolytic degradation product
?
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x * 60000 and x * 63000, SDS-PAGE
?
x * 47850, sequence calculation
?
x * 53680, sequence calculation
?
x * 54890, sequence calculation
?
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x * 61200, SDS-PAGE under reducing conditions
?
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x * 57000, SDS-PAGE, immunoprecipitation
?
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x * 58000, recombinant ECaSt/PDI, SDS-PAGE
?
x * 27700, ERp27, SDS-PAGE
?
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x * 53100, oxidized enzyme, calculated from amino acid sequence
?
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x * 58800, reduced enzyme, small-angle X-ray scattering
?
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x * 66400, oxidized enzyme, small-angle X-ray scattering
?
x * 15000, isozyme pdi-15, SDS-PAGE
?
x * 40000, isozyme pdi-40, SDS-PAGE
?
x * 47000, isozyme pdi-47, SDS-PAGE
?
x * 52000, isozyme pdi-52, SDS-PAGE
?
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x * 65000, recombinant mature PDILT without signal sequence, SDS-PAGE
?
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x * 52000, native enzyme, SDS-PAGE, x * 55000, recombinant His-tagged enzyme, SDS-PAGE
?
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x * 55000, recombinant His-tagged enzyme, SDS-PAGE
?
x * 55000, recombinant PDI, SDS-PAGE, x * 85000, recombinant GST-tagged PDI, SDS-PAGE
?
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x * 55114, calculation from nucleotide sequence
?
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x * 58900, SDS-PAGE under reducing conditions, other bands with MW 53800 and 55200 represent proteolytic degradation products of the 58900 MW protein
?
x * 26032, calculated from sequence
?
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x * 26032, calculated from sequence
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?
x * 52800, calculated from amino acid sequence
?
x * 39490, sequece calculation
?
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x * 39490, sequece calculation
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?
x * 48074, PDI-P5, sequence calculation, x * 56859, PDIA3, sequence calculation
?
x * 40000, isoform PDIL4D, SDS-PAGE
?
x * 47000, isoform PDIL5A, SDS-PAGE
?
x * 60000, isoform PDIL1Aalpha, SDS-PAGE
?
x * 60000, isoform PDIL1B, SDS-PAGE
?
x * 69000, isoform PDIL3A, SDS-PAGE
?
x * 70000, isoform PDIL2, SDS-PAGE
?
x * 45000, recombinant PDI-1, SDS-PAGE, x * 80000, recombinant PDI-2, SDS-PAGE
dimer
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dimer
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2 * 57000, SDS-PAGE
dimer
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2 * 57000, SDS-PAGE under reducing and nonreducing conditions, association between subunits is noncovalent
dimer
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2 * 60000, SDS-PAGE
dimer
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DsbC contains an N-terminal dimerization domain followed by a linker helix both involved in protein dimerization, the linker helix helps separate the C-terminal catalytic domains
dimer
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DsbC dimerizes to form a protein binding site flanked by two catalytic thioredoxin domains
dimer
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DsbG is a homodimer with an N-terminal dimerization domain on each subunit, crystal structure
dimer
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V-shaped homodimeric modular structures of the dimerization domains and dimer interface of DsbC and DsbG, the dimerization domains fold independently of the catalytic portions of the full-length molecules, overview, each dimeric molecule contains two separate C-terminal thioredoxin-fold domains, joined by hinged helical stalks to a single N-terminal dimerization domain formed from the N-terminal 67 residues of each monomer
dimer
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2 * 63000, SDS-PAGE
dimer
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2 * 60000, SDS-PAGE
dimer
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and monomer. 2 * 62000, gel filtration, 2 * 56000, calculated
dimer
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2 * 22000, DsbA, SDS-PAGE, 2 * 25000, DsbC, SDS-PAGE
dimer
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2 * 55000, about, sequence calculation, 2 * 52000, analytical ultrafiltration
dimer
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2 * 55000, SDS-PAGE
dimer
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2 * 70000, SDS-PAGE
dimer
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crystallization data
monomer
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1 * 21100, estimated from amino acid sequence
monomer
1 * 64000, analytical ultracentrifugation
monomer
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1 * 56300, calculated from amino acid sequence
monomer
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1 * 57700, analytical ultracentrifugation
monomer
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and dimer. 1 * 62000, gel filtration, 1 * 56000, calculated
monomer
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predominantly, isozyme PDI-22, SDS-PAGE and gel filtration
additional information
domain organization of PDI, overview
additional information
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domain organization of PDI, overview
additional information
CYO1 has a C4-type zinc finger domain, putative enzyme topology, overview
additional information
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CYO1 has a C4-type zinc finger domain, putative enzyme topology, overview
additional information
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PDI domain structure, overview
additional information
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PDI domain organization, overview
additional information
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a multidomain protein, tertiary structure and function analysis under pressure conditions above 100 MPa, overview
additional information
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isozyme domain structure, overview
additional information
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PDI domain structure, overview
additional information
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tryptic peptide preparation and analysis by MALDI-MS/MS and LC-ESI-MS/MS methods, peptide mapping and amino acid sequence determination, sequence comparison, overview
additional information
formation of an intramolecular disulfide bond Cys21-Cys24 in the enzyme structure under oxidative stress
additional information
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formation of an intramolecular disulfide bond Cys21-Cys24 in the enzyme structure under oxidative stress
additional information
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formation of an intramolecular disulfide bond Cys21-Cys24 in the enzyme structure under oxidative stress
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additional information
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formation of an intramolecular disulfide bond Cys21-Cys24 in the enzyme structure under oxidative stress
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additional information
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formation of an intramolecular disulfide bond Cys21-Cys24 in the enzyme structure under oxidative stress
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additional information
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formation of an intramolecular disulfide bond Cys21-Cys24 in the enzyme structure under oxidative stress
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additional information
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formation of an intramolecular disulfide bond Cys21-Cys24 in the enzyme structure under oxidative stress
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additional information
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formation of an intramolecular disulfide bond Cys21-Cys24 in the enzyme structure under oxidative stress
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additional information
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protein disulfide isomerase-related chaperone Wind contains a thioredoxin fold domain and a C-terminal D-domain unique in PDI-D proteins
additional information
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PDI domain organization, overview
additional information
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the catalytic domain, residues 88-231, shows a thioredoxin fold with a helical insert
additional information
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PDI domain structure, overview
additional information
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the enzyme structure contains two thioredoxin-like domains, a and a', and an ERp29c domain, determination by peptide mapping with either trypsin or V8 protease, domain structures, overview
additional information
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isoform PDIL-1 associates with the precursor of a seed storage protein, proglycinin, and with the alpha' subunit of the seed storage protein beta-conglycinin
additional information
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isoform PDIL-2 associates with the precursor of a seed storage protein, proglycinin, and with the alpha' subunit of the seed storage protein beta-conglycinin
additional information
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GmPDIL-3a and GmPDIL-3b are plant endoplasmic reticulum PDI family proteins containing the nonclassic redox center motif CXXS? C
additional information
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PDI consist of 2 catalytically active domains, a and a', and two inactive ones b and b', all four domains have a thioredoxin fold, domain b' contains he primary peptide binding site
additional information
PDI is a multifunctional enzyme that acts as beta subunit in prolyl 4-hydroxylases and as a subunit in the microsomal triglyceride transfer protein
additional information
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PDI domain organization, 5 domains a, b, b', a', and c, the acidic C-terminal domain c, residues 463-491, stabilizes the chaperone function of the enzyme
additional information
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PDI domain organization, domains a, b, b', a', PDI and P5 contain both two thioredoxin-like domains, domains a and a', at the N-terminus and the C-terminus, respectively, are homologous to thioredoxin and both have an independent active site, each active site contains 2 cysteine residues within the sequence WCGHCK, overview
additional information
the four domains a, b, b', and a' are arranged in an annular manner
additional information
determination and analysis of the crystal structure of the bb domains of ERp57, overview
additional information
domain structure of isozymes, comparison, overview
additional information
domain structure of isozymes, comparison, overview
additional information
domain structure of isozymes, comparison, overview
additional information
domain structure of isozymes, comparison, overview
additional information
ERp27 is a two-domain protein homologous to the non-catalytic b and b' domains of protein disulfide isomerase, domain structure, thioredoxin site structure and involved residues, overview
additional information
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ERp27 is a two-domain protein homologous to the non-catalytic b and b' domains of protein disulfide isomerase, domain structure, thioredoxin site structure and involved residues, overview
additional information
PDI domain structure, overview
additional information
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PDI can directly interact with estrogen receptor alpha, but it does not interact with estrogen receptor beta
additional information
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PDIp exists predominantly as monomer under reducing conditions, but the dimeric form is significantly increased following the removal of the reducing agent, due to the formation of an inter-subunit disulfide bond. The oxidized PDIp exposes more hydrophobic patches and is more sensitive to protease digestion. The formation of the inter-subunit disulfide bond is mainly contributed by its non-active cysteine residue C4. The formation of the inter-subunit disulfide bond is redox-dependent and is favored under oxidizing conditions. PDIp can function as a chaperone to form stable complexes with various non-native cellular proteins, particularly under oxidizing conditions
additional information
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reconstitution of the Ero1-Lalpha/protein disulfide isomerase oxidative folding system in vitro. The a' domain of protein disulfide isomerase is much more active than the a domain in Ero1-Lalpha-mediated folding. The minimal element for binding to Ero1-Lalpha are core element b, linker x and the a domain
additional information
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the enzyme molecule has four domains a,a', b, and b', each possessing a thioredoxin fold, the domain a and a' show catalytic sites with the Cys-Gly-His-Cys motif, the b and b' domains possess substrate binding sites, domains b' and a' are linked via linker x, and the enbzyme also posseses a C-terminal acidic alpha-helix containing the endoplasmic reticulum retention signal, domain structure, overview
additional information
the protein disulfide isomerase exhibits a saturable, substrate binding site. NMR structural analysis of peptide binding pocket of b and b' domains, and interaction analysis of b and b' domains of PDI, the b' domain tends to form dimers, while the b domain moderates the tendency of the b' domain to dimerize and significantly slows interconversion, overview
additional information
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the protein disulfide isomerase exhibits a saturable, substrate binding site. NMR structural analysis of peptide binding pocket of b and b' domains, and interaction analysis of b and b' domains of PDI, the b' domain tends to form dimers, while the b domain moderates the tendency of the b' domain to dimerize and significantly slows interconversion, overview
additional information
the two catalytic domains of PDIp, a and a', which contain the WCGHC and WCTHC motifs, respectively, may be responsible for its enzymatic activity, whereas the two non-catalytic domains, b and b', may be involved in substrate-binding
additional information
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the two catalytic domains of PDIp, a and a', which contain the WCGHC and WCTHC motifs, respectively, may be responsible for its enzymatic activity, whereas the two non-catalytic domains, b and b', may be involved in substrate-binding
additional information
the enzyme has a modular structure with four thioredoxin-like domains, a, b, b', and a', along with a C-terminal extension. The homologous a and a' domains contain one cysteine pair in their active site directly involved in thiol-disulfide exchange reactions, while the b' domain putatively provides a primary binding site for unstructured regions of the substrate polypeptides, structure determination and analysis by NMR and small-angle X-ray scattering methods, domain arrangements and redox behaviour, overview
additional information
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the enzyme has a modular structure with four thioredoxin-like domains, a, b, b', and a', along with a C-terminal extension. The homologous a and a' domains contain one cysteine pair in their active site directly involved in thiol-disulfide exchange reactions, while the b' domain putatively provides a primary binding site for unstructured regions of the substrate polypeptides, structure determination and analysis by NMR and small-angle X-ray scattering methods, domain arrangements and redox behaviour, overview
additional information
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the enzyme molecule has four domains a,a', b, and b', each possessing a thioredoxin fold, the domain a and a' show catalytic sites with the Cys-Gly-His-Cys motif, the b and b' domains possess substrate binding sites, domains b' and a' are linked via linker x, and the enbzyme also posseses a C-terminal acidic alpha-helix containing the endoplasmic reticulum retention signal, domain structure, overview
additional information
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primary and secondary PDi structure analysis, overview
additional information
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in solution at low concentration, enzyme comprises mainly monomers. At increasing concentrations, fractions of dimers and higher order oligomers are observed. Oligomerization is not driven by formation of intermolecular disulfide bonds, but by non-covalent interactions
additional information
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structural analysis and comparison of PDIs from different Plasmodium species
additional information
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structural analysis and comparison of PDIs from different Plasmodium species
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additional information
structure determination and molecular modeling, overview
additional information
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structure determination and molecular modeling, overview
additional information
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structural analysis and comparison of PDIs from different Plasmodium species
additional information
structural analysis and comparison of PDIs from different Plasmodium species
additional information
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structural analysis and comparison of PDIs from different Plasmodium species
additional information
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structural analysis and comparison of PDIs from different Plasmodium species
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additional information
structural analysis and comparison of PDIs from different Plasmodium species
additional information
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structural analysis and comparison of PDIs from different Plasmodium species
additional information
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structural analysis and comparison of PDIs from different Plasmodium species
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additional information
structural analysis and comparison of PDIs from different Plasmodium species
additional information
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structural analysis and comparison of PDIs from different Plasmodium species
additional information
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PDI domain organization, 5 domains a, b, b', a', and c, domains a and a' are homologous to thioredoxin and both have an independent active site, each active site contains 2 cysteine residues within the sequence WCGHCK, domain structure and electrostatic surface, overview
additional information
comparison of structures of b and b' domains and the bb' fragments of ERp57 and ERp72, modelling, overview
additional information
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comparison of structures of b and b' domains and the bb' fragments of ERp57 and ERp72, modelling, overview
additional information
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the enzyme molecule has four domains a,a', b, and b', each possessing a thioredoxin fold, the domain a and a' show catalytic sites with the Cys-Gly-His-Cys motif, the b and b' domains possess substrate binding sites, domains b' and a' are linked via linker x, and the enzyme also posseses a C-terminal acidic alpha-helix containing the endoplasmic reticulum retention signal, domain structure, overview
additional information
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domain arrangement: two catalytically inactive thioredoxin domains inserted between two catalytically active thioredoxin domains and an acidic C-terminal tail, the four thioredoxin domains form the shape of a twisted U with the active sites facing each other across the long sides, the inside surface is enriched in hydrophobic residues facilitating interactions with misfolded proteins, all 5 domains of PDI are required for full catalytic activity
additional information
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non-active site cysteines form a disulfide bridge that is stable even under very reducing environment destabilizing the N-terminal active site disulfide which becomes a 18fold better oxidant by this way
additional information
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PDI domain organization, Eug1p, Mpd1p, Mpd2p, and Eps1p have only one catalytic domain with 2 cysteines, overview
additional information
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the catalytic domains a and a' are responsible for the oxidase and the isomerase activity, respectively
additional information
PDI domain structure, overview
additional information
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PDI domain structure, overview
additional information
the PDIA3 sequence contains two PDI-typical thioredoxin active sites of WCGHC
additional information
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the PDIA3 sequence contains two PDI-typical thioredoxin active sites of WCGHC