1pys
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(New page: 200px<br /><applet load="1pys" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pys, resolution 2.9Å" /> '''PHENYLALANYL-TRNA SYN...)
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Revision as of 22:07, 20 November 2007
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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 with MG as ligand. Active as Phenylalanine--tRNA ligase, with EC number 6.1.1.20 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
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