1v7o
Alanyl-tRNA synthetase editing domain homologue protein from Pyrococcus horikoshiiAlanyl-tRNA synthetase editing domain homologue protein from Pyrococcus horikoshii
Structural highlights
FunctionALAXS_PYRHO Functions in trans to edit the amino acid moiety from mischarged charged Ser-tRNA(Ala). Has little activity against Gly-tRNA(Ala). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedAlaX 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). 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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