1obc
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(New page: 200px<br /> <applet load="1obc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1obc, resolution 2.10Å" /> '''LEUCYL-TRNA SYNTHET...)
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Revision as of 15:25, 29 October 2007
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LEUCYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH A POST-TRANSFER EDITING SUBSTRATE ANALOGUE
Overview
The aminoacyl-tRNA synthetases link tRNAs with their cognate amino acid., In some cases, their fidelity relies on hydrolytic editing that destroys, incorrectly activated amino acids or mischarged tRNAs. We present, structures of leucyl-tRNA synthetase complexed with analogs of the, distinct pre- and posttransfer editing substrates. The editing active site, binds the two different substrates using a single amino acid, discriminatory pocket while preserving the same mode of adenine, recognition. This suggests a similar mechanism of hydrolysis for both, editing substrates that depends on a key, completely conserved aspartic, acid, which interacts with the alpha-amino group of the noncognate amino, acid and positions both substrates for hydrolysis. Our results demonstrate, the economy by ... [(full description)]
About this Structure
1OBC is a [Single protein] structure of sequence from [Thermus thermophilus] with ZN, LEU and LMS as [ligands]. Full crystallographic information is available from [OCA].
Reference
Structural and mechanistic basis of pre- and posttransfer editing by leucyl-tRNA synthetase., Lincecum TL Jr, Tukalo M, Yaremchuk A, Mursinna RS, Williams AM, Sproat BS, Van Den Eynde W, Link A, Van Calenbergh S, Grotli M, Martinis SA, Cusack S, Mol Cell. 2003 Apr;11(4):951-63. PMID:12718881[[Category: atp + l-leucine + trna (leu) -> amp + ppi l-leucyl-trna(leu)]]
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