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1h3n
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(New page: 200px<br /> <applet load="1h3n" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h3n, resolution 2.00Å" /> '''LEUCYL-TRNA SYNTHET...)
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Revision as of 17:16, 29 October 2007
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LEUCYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH A SULPHAMOYL ANALOGUE OF LEUCYL-ADENYLATE
Overview
Leucyl-, isoleucyl- and valyl-tRNA synthetases are closely related large, monomeric class I synthetases. Each contains a homologous insertion domain, of approximately 200 residues, which is thought to permit them to, hydrolyse ('edit') cognate tRNA that has been mischarged with a chemically, similar but non-cognate amino acid. We describe the first crystal, structure of a leucyl-tRNA synthetase, from the hyperthermophile Thermus, thermophilus, at 2.0 A resolution. The overall architecture is similar to, that of isoleucyl-tRNA synthetase, except that the putative editing domain, is inserted at a different position in the primary structure. This feature, is unique to prokaryote-like leucyl-tRNA synthetases, as is the presence, of a novel additional flexibly inserted domain. Comparison of ... [(full description)]
About this Structure
1H3N is a [Single protein] structure of sequence from [Thermus thermophilus] with ZN, SO4 and LEU as [ligands]. Full crystallographic information is available from [OCA].
Reference
The 2 A crystal structure of leucyl-tRNA synthetase and its complex with a leucyl-adenylate analogue., Cusack S, Yaremchuk A, Tukalo M, EMBO J. 2000 May 15;19(10):2351-61. PMID:10811626[[Category: atp + l-leucine + trna (leu) -> amp + ppi + l-leucyl-trna(leu)]]
Page seeded by OCA on Mon Oct 29 19:20:51 2007
