1v7o: Difference between revisions

Revision as of 15:03, 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:1v7o.png

Template:STRUCTURE 1v7o

Alanyl-tRNA synthetase editing domain homologue protein from Pyrococcus horikoshiiAlanyl-tRNA synthetase editing domain homologue protein from Pyrococcus horikoshii

Template:ABSTRACT PUBMED 16087889

About this StructureAbout this Structure

1V7O is a Single protein structure of sequence from Pyrococcus horikoshii. Full crystallographic information is available from OCA.

ReferenceReference

Molecular basis of alanine discrimination in editing site., Sokabe M, Okada A, Yao M, Nakashima T, Tanaka I, Proc Natl Acad Sci U S A. 2005 Aug 16;102(33):11669-74. Epub 2005 Aug 8. PMID:16087889

Page seeded by OCA on Sun Jul 27 15:03:46 2008

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OCA

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-'''Alanyl-tRNA synthetase editing domain homologue protein from Pyrococcus horikoshii'''
+===Alanyl-tRNA synthetase editing domain homologue protein from Pyrococcus horikoshii===
-==Overview==
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-AlaX is the homologue of the class II alanyl-tRNA synthetase editing domain and has been shown to exhibit autonomous editing activity against mischarged tRNA(Ala). Here, we present the structures of AlaX from the archaeon Pyrococcus horikoshii in apo form, complexed with zinc, and with noncognate amino acid l-serine and zinc. Together with mutational analysis, we demonstrated that the conserved Thr-30 hydroxyl group located near the beta-methylene of the bound serine is responsible for the discrimination of noncognate serine from cognate alanine, based on their chemical natures. Furthermore, we confirmed that the conserved Gln-584 in alanyl-tRNA synthetase, which corresponds to Thr-30 of AlaX, is also critical for discrimination. These observations strongly suggested conservation of the chemical discrimination among trans- and cis-editing of tRNA(Ala).
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 [[Category: Yao, M.]]
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