2X1L

Crystal structure of Mycobacterium smegmatis methionyl-tRNA synthetase in complex with methionine and adenosine

2X1L の概要

• エントリーDOI: 10.2210/pdb2x1l/pdb
• 関連するPDBエントリー: 2X1M
• 分子名称: METHIONYL-TRNA SYNTHETASE, METHIONINE, ADENOSINE, ... (6 entities in total)
• 機能のキーワード: nucleotide-binding, protein biosynthesis, ligase, aminoacyl-trna synthetase
• 由来する生物種: MYCOBACTERIUM SMEGMATIS
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 179729.91

構造登録者

Ingvarsson, H.,Jones, T.A.,Unge, T. (登録日: 2009-12-31, 公開日: 2010-07-28, 最終更新日: 2023-12-20)

主引用文献

Ingvarsson, H.,Unge, T.
Flexibility and Communication within the Structure of the Mycobacterium Smegmatis Methionyl-tRNA Synthetase.
FEBS J., 277:3947-, 2010

PubMed Abstract: Two structures of monomeric methionyl-tRNA synthetase, from Mycobacterium smegmatis, in complex with the ligands methionine/adenosine and methionine, were analyzed by X-ray crystallography at 2.3 Å and at 2.8 Å, respectively. The structures demonstrated the flexibility of the multidomain enzyme. A new conformation of the structure was identified in which the connective peptide domain bound more closely to the catalytic domain than described previously. The KMSKS(301-305) loop in our structures was in an open and inactive conformation that differed from previous structures by a rotation of the loop of about 90° around hinges located at Asn297 and Val310. The binding of adenosine to the methionyl-tRNA synthetase methionine complex caused a shift in the KMSKS domain that brought it closer to the catalytic domain. The potential use of the adenosine-binding site for inhibitor binding was evaluated and a potential binding site for a specific allosteric inhibitor was identified.

PubMed: 20796028
DOI: 10.1111/J.1742-4658.2010.07784.X

実験手法

X-RAY DIFFRACTION (2.3 Å)