1pys: Difference between revisions

Revision as of 14:16, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1pys.png

Template:STRUCTURE 1pys

PHENYLALANYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUSPHENYLALANYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS

Template:ABSTRACT PUBMED 7664121

About this StructureAbout this Structure

1PYS is a Protein complex structure of sequences from Thermus thermophilus. Full crystallographic information is available from OCA.

ReferenceReference

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

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OCA

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-'''PHENYLALANYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS'''
+===PHENYLALANYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS===
-==Overview==
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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.
+The line below this paragraph, {{ABSTRACT_PUBMED_7664121}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7664121 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_7664121}}
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 [[Category: Sh3 domain]]
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