1WXO

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

1WXO の概要

• エントリーDOI: 10.2210/pdb1wxo/pdb
• 関連するPDBエントリー: 1V7O 1WNU
• 分子名称: alanyl-tRNA synthetase, ZINC ION (3 entities in total)
• 機能のキーワード: hydrolase, trans-editing
• 由来する生物種: Pyrococcus horikoshii
• 細胞内の位置: Cytoplasm (Probable): O58307
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 54745.40

構造登録者

Sokabe, M.,Okada, A.,Nakashima, T.,Yao, M.,Tanaka, I. (登録日: 2005-01-27, 公開日: 2005-07-26, 最終更新日: 2023-10-25)

主引用文献

Sokabe, 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

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

実験手法

X-RAY DIFFRACTION (1.88 Å)