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1pys
From Proteopedia
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'''PHENYLALANYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS''' | '''PHENYLALANYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS''' | ||
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[[Category: Reshetnikova, L.]] | [[Category: Reshetnikova, L.]] | ||
[[Category: Safro, M.]] | [[Category: Safro, M.]] | ||
| - | [[Category: | + | [[Category: Class ii aminoacyl-trna synthetase]] |
| - | [[Category: | + | [[Category: Helix-turn-helix motif]] |
| - | [[Category: | + | [[Category: Phenylalanyl-trna synthetase]] |
| - | [[Category: | + | [[Category: Rbd domain]] |
| - | [[Category: | + | [[Category: Sh3 domain]] |
| - | [[Category: | + | [[Category: Thermus thermophilus]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:39:20 2008'' | |
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Revision as of 02:39, 3 May 2008
PHENYLALANYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS
Overview
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.
About this Structure
1PYS is a Protein complex structure of sequences from Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus., Mosyak L, Reshetnikova L, Goldgur Y, Delarue M, Safro MG, Nat Struct Biol. 1995 Jul;2(7):537-47. PMID:7664121 Page seeded by OCA on Sat May 3 05:39:20 2008
