1wnu

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spinqualitylabelsall models 1wnu, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Structure of Archaeal Trans-Editing Protein AlaX in complex with L-serine

Overview

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).

About this Structure

1WNU is a Single protein structure of sequence from Pyrococcus horikoshii with ZN and SER as ligands. Full crystallographic information is available from OCA.

Reference

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

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