1MKH

C-terminal domain of methionyl-tRNA synthetase from Pyrococcus abyssi

1MKH の概要

• エントリーDOI: 10.2210/pdb1mkh/pdb
• 分子名称: C-terminal domain of Methionyl-tRNA synthetase (2 entities in total)
• 機能のキーワード: beta barrel, dimerization domain, ligase
• 由来する生物種: Pyrococcus abyssi
• 細胞内の位置: Cytoplasm: Q9V011
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12062.24

構造登録者

Crepin, T.,Schmitt, E.,Blanquet, S.,Mechulam, Y. (登録日: 2002-08-29, 公開日: 2003-02-04, 最終更新日: 2024-02-14)

主引用文献

Crepin, T.,Schmitt, E.,Blanquet, S.,Mechulam, Y.
Structure and function of the C-terminal domain of methionyl-tRNA synthetase
Biochemistry, 41:13003-13011, 2002

PubMed Abstract: The minimal polypeptide supporting full methionyl-tRNA synthetase (MetRS) activity is composed of four domains: a catalytic Rossmann fold, a connective peptide, a KMSKS domain, and a C-terminal alpha helix bundle domain. The minimal MetRS behaves as a monomer. In several species, MetRS is a homodimer because of a C-terminal domain appended to the core polypeptide. Upon truncation of this C-terminal domain, subunits dissociate irreversibly. Here, the C-terminal domain of dimeric MetRS from Pyrococcus abyssi was isolated and studied. It displays nonspecific tRNA-binding properties and has a crystalline structure closely resembling that of Trbp111, a dimeric tRNA-binding protein found in many bacteria and archaea. The obtained 3D model was used to direct mutations against dimerization of Escherichia coli MetRS. Comparison of the resulting mutants to native and C-truncated MetRS shows that the presence of the appended C-domain improves tRNA(Met) binding affinity. However, dimer formation is required to evidence the gain in affinity.

PubMed: 12390027
DOI: 10.1021/bi026343m

実験手法

X-RAY DIFFRACTION (2.01 Å)