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1WXO

Structure of Archaeal Trans-Editing Protein AlaX in complex with zinc

Summary for 1WXO
Entry DOI10.2210/pdb1wxo/pdb
Related1V7O 1WNU
Descriptoralanyl-tRNA synthetase, ZINC ION (3 entities in total)
Functional Keywordshydrolase, trans-editing
Biological sourcePyrococcus horikoshii
Cellular locationCytoplasm (Probable): O58307
Total number of polymer chains3
Total formula weight54745.40
Authors
Sokabe, M.,Okada, A.,Nakashima, T.,Yao, M.,Tanaka, I. (deposition date: 2005-01-27, release date: 2005-07-26, Last modification date: 2023-10-25)
Primary citationSokabe, M.,Okada, A.,Yao, M.,Nakashima, T.,Tanaka, I.
Molecular basis of alanine discrimination in editing site
Proc.Natl.Acad.Sci.Usa, 102:11669-11674, 2005
Cited by
PubMed Abstract: 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).
PubMed: 16087889
DOI: 10.1073/pnas.0502119102
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.88 Å)
Structure validation

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