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x * 59000 (alpha) + x * 72000 (beta)
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x * 74000 (alpha) + x * 63000 (beta), SDS-PAGE
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x * 60000, alpha-subunit, + x * 70000, beta-subunit, SDS-PAGE
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x * 57600, alpha-subunit, + x * 66200, beta-subunit, amino acid sequence determination
dimer
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dimer
1 * 55000, alpha-subunit, + 1 * 57000, beta-subunit, alphabeta, amino acid determination
dimer
1 * 55000, alpha-subunit, + 1 * 57000, beta-subunit, alphabeta2, amino acid determination
dimer
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1 * 33000 (alpha) + 1 * 42000 (beta), SDS-PAGE
heterodimer
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1 * 54000, alpha-subunit, + 1 * 62000, beta-subunit, SDS-PAGE
heterodimer
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1 * 80000 + 1 * 41000, SDS-PAGE
heterodimer
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1 * 85000 + 1 * 42000, SDS-PAGE
heterotetramer
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EcPheRS, alpha and beta-subunits, the alpha-subunits contain the actice site, the beta-subunits harbor the editing site
heterotetramer
EcPheRS is a (alphabeta)2 heterotetramer, built of two alphabeta heterodimers
heterotetramer
build of two alphabeta heterodimers
heterotetramer
two alpha and two beta subunits
heterotetramer
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ctPheRS, alpha and beta-subunits, the alpha-subunits contain the actice site, the beta-subunits harbor the editing site
monomer
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monomer
1 * 48000, recombinant mitochondrial isozyme, analytical sedimentation centrifugation
monomer
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1 * 48000, recombinant enzyme, SDS-PAGE
monomer
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1 * 49600, sequence calculation
monomer
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mtPheRS, alpha-subunit monomer, catalytic domain
oligomer
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PheRs is a multidomain (alphabeta)2 heterotetrameric protein, the alpha subunit forms the catalytic core of the enzyme, while the beta subunit contains a number of autonomous structural modules with a wide range of functions including tRNA anticodon binding and editing of the misaminoacylated species Tyr-tRNAPhe
oligomer
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PheRs is a multidomain (alphabeta)2 heterotetrameric protein, the alpha subunit forms the catalytic core of the enzyme, while the beta subunit contains a number of autonomous structural modules with a wide range of functions including tRNA anticodon binding and editing of the misaminoacylated species Tyr-tRNAPhe
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tetramer
2 * alpha + 2 * beta
tetramer
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2 * alpha + 2 * beta
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tetramer
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2 * 39000 (alpha) + 2 * 94000 (beta), SDS-PAGE
tetramer
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2 * 98000 (alpha) + 2 * 38000 (beta), SDS-PAGE
tetramer
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2 * 39000 (alpha) + 2 * 94000 (beta), SDS-PAGE
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tetramer
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2 * 57000 (alpha) + 2 * 66000 (beta), SDS-PAGE
tetramer
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2 * 57000, alpha-subunit, + 2 * 66000, beta-subunit, (alphabeta)2, SDS-PAGE
tetramer
Methanobacterium thermoautotrophicus
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2 * 60000, alpha, + 2 * 70000, beta, alphabeta2, SDS-PAGE
tetramer
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2 * 63000 (alpha) + 2 * 70000 (beta), SDS-PAGE
tetramer
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2 * 59000 (alpha) + 2 * 70000 (beta), PAGE under denaturing conditions
tetramer
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PheRS belongs to class IIc and is a tetrameric enzyme consisting of two alphabeta heterodimers. The B3/4 domain of the beta-subunit catalyzes the editing, domain architecture, overview
tetramer
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2 * 56000, alpha-subunit, + 2 * 64000, beta-subunit, (alphabeta)2, SDS-PAGE
tetramer
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2 * 57000 (alpha) + 2 * 72000 (beta), urea-SDS PAGE
tetramer
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2 * 40000, alpha subunit, + 2 * 90000, beta-subunit, (alphabeta)2, recombinant enzyme, SDS-PAGE
tetramer
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2 * 40000 (alpha) + 2 * 92000 (beta), SDS-PAGE
tetramer
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(alphabeta)2 heterotetramer
additional information
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the separated subunits do not possess any detectable tRNA-amino-acylation activity
additional information
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the separated subunits do not possess any detectable tRNA-amino-acylation activity
additional information
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all forms of homologous subunits have no catalytic activity
additional information
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beta-subunits exist in solution mainly in the monomeric form with negligible formation of beta2-dimers. The alpha-subunits predominantly form alpha2-dimers
additional information
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beta-subunits exist in solution mainly in the monomeric form with negligible formation of beta2-dimers. The alpha-subunits predominantly form alpha2-dimers
additional information
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the tRNA-binding sites are formed on heavy beta-subunits of the enzyme. The catalytic center of tRNA aminoacylation is formed in the contact region of subunits
additional information
EcPheRS consists of 11 structural domains. Three of them: the N-terminus, A1 and A2 belong to the alpha-subunit and B1-B8 domains to the beta subunit. The N-terminal domain of the alpha-subunit in EcPheRS forms compact triple helix domain, structure comparisons, overview
additional information
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EcPheRS consists of 11 structural domains. Three of them: the N-terminus, A1 and A2 belong to the alpha-subunit and B1-B8 domains to the beta subunit. The N-terminal domain of the alpha-subunit in EcPheRS forms compact triple helix domain, structure comparisons, overview
additional information
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the separated subunits do not possess any detectable tRNA-amino-acylation activity
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additional information
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beta-subunits exist in solution mainly in the monomeric form with negligible formation of beta2-dimers. The alpha-subunits predominantly form alpha2-dimers
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additional information
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the tRNA-binding sites are formed on heavy beta-subunits of the enzyme. The catalytic center of tRNA aminoacylation is formed in the contact region of subunits
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additional information
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enzyme is part of an aminoacyl-tRNA synthetase complex which is resistant to dissociation when subjected to gel filtration
additional information
the catalytic function resides in the alpha-subunit, while the beta-subunit provides several binding-like domains for OB, RNP, SH3, and DNA
additional information
the catalytic function resides in the alpha-subunit, while the beta-subunit provides several binding-like domains for OB, RNP, SH3, and DNA
additional information
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the catalytic function resides in the alpha-subunit, while the beta-subunit provides several binding-like domains for OB, RNP, SH3, and DNA
additional information
the mitochondrial isozyme is a single polypeptide chain, which bears similarities in structure to the alpha/beta subunit organization of bacterial enzymes
additional information
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the mitochondrial isozyme is a single polypeptide chain, which bears similarities in structure to the alpha/beta subunit organization of bacterial enzymes
additional information
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human mitPheRS is a chimera of the bacterial beta-subunit of PheRS and the B8 domain of its beta-subunit, together, the beta-subunit and the RNP-domain, i.e. B8 domain, at the C-terminus form the minimal structural set to construct an enzyme with phenylalanylation activity, overview
additional information
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human mitPheRS consists of four major parts: the N-terminal region, residues 1-47, the catalytic domain, residues 48-289, the linker region, residues 290-322, and the C-terminal domain, residues 323-415. Multimeric organization is not a prerequisite for phenylalanylation activity, as monomeric mitochondrial phenylalanyl-tRNA synthetase is also active. The anticodon binding domain of the beta subunit of alphabeta2 PheRS is located at the C-terminus of mitPheRS overlapping with the acceptor stem of phenylalanine transfer RNA, structure, overview
additional information
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structure molecular dynamics simulations of hmtPheRS, wild-type and mutant enzymes, overview
additional information
the N-terminal fragment of the PheRS beta-subunit includes the editing domain B3/4, which has archaea/eukarya-specific insertions/deletions and adopts a different orientation relative to other domains, as compared with that of bacterial PheRS, structure, overview
additional information
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the N-terminal fragment of the PheRS beta-subunit includes the editing domain B3/4, which has archaea/eukarya-specific insertions/deletions and adopts a different orientation relative to other domains, as compared with that of bacterial PheRS, structure, overview
additional information
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the amino terminal part of each beta-subunit represents the main tRNA binding domain and is not involved in either catalysis or subunit interactions. The trypsin resistant alpha2beta2 core contains the catalytic site as well as contact areas between subunits
additional information
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structure analysis and structure-activity relationship, overview
additional information
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the separated subunits do not possess any detectable tRNA-amino-acylation activity
additional information
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the separated subunits do not possess any detectable tRNA-amino-acylation activity
additional information
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all forms of homologous subunits have no catalytic activity
additional information
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both alpha- and beta-subunits mainly exist in the dimeric form
additional information
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alphabeta organization, the alpha-subunit is the catalytically active one
additional information
the enzyme is modularly composed of several different domains
additional information
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the enzyme is modularly composed of several different domains
additional information
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the separated subunits do not possess any detectable tRNA-amino-acylation activity
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additional information
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both alpha- and beta-subunits mainly exist in the dimeric form
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