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PDBsum entry 1pys
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Aminoacyl-tRNA synthetase
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PDB id
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1pys
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structure of phenylalanyl-Trna synthetase from thermus thermophilus.
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Authors
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L.Mosyak,
L.Reshetnikova,
Y.Goldgur,
M.Delarue,
M.G.Safro.
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Ref.
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Nat Struct Biol, 1995,
2,
537-547.
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PubMed id
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Abstract
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The crystal structure of phenylalanyl-tRNA synthetase from Thermus thermophilus,
solved at 2.9 A resolution, displays (alpha beta)2 subunit organization.
Unexpectedly, both the catalytic alpha- and the non-catalytic beta-subunits
comprise the characteristic fold of the class II active-site domains. The alpha
beta heterodimer contains most of the building blocks so far identified in the
class II synthetases. The presence of an RNA-binding domain, similar to that of
the U1A spliceosomal protein, in the beta-subunit is indicative of structural
relationships among different families of RNA-binding proteins. The structure
suggests a plausible catalytic mechanism which explains why the primary site of
tRNA aminoacylation is different from that of the other class II enzymes.
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