3TD2

Crystal structures of Peptidyl-tRNA hydrolase from Mycobacterium tuberculosis - Form 5

3TD2 の概要

• エントリーDOI: 10.2210/pdb3td2/pdb
• 関連するPDBエントリー: 3TCK 3TCN 3TD6
• 分子名称: Peptidyl-tRNA hydrolase (2 entities in total)
• 機能のキーワード: pth, hydrolysis of peptidyl-trna, peptidyl-trna, cytosol, hydrolase
• 由来する生物種: Mycobacterium tuberculosis
• 細胞内の位置: Cytoplasm (By similarity): P65865
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20485.53

構造登録者

Selvaraj, M.,Ahmad, R.,Varshney, U.,Vijayan, M. (登録日: 2011-08-10, 公開日: 2012-02-15, 最終更新日: 2023-11-01)

主引用文献

Selvaraj, M.,Ahmad, R.,Varshney, U.,Vijayan, M.
Structures of new crystal forms of Mycobacterium tuberculosis peptidyl-tRNA hydrolase and functionally important plasticity of the molecule
Acta Crystallogr.,Sect.F, 68:124-128, 2012

PubMed Abstract: The X-ray structures of new crystal forms of peptidyl-tRNA hydrolase from M. tuberculosis reported here and the results of previous X-ray studies of the enzyme from different sources provide a picture of the functionally relevant plasticity of the protein molecule. The new X-ray results confirm the connection deduced previously between the closure of the lid at the peptide-binding site and the opening of the gate that separates the peptide-binding and tRNA-binding sites. The plasticity of the molecule indicated by X-ray structures is in general agreement with that deduced from the available solution NMR results. The correlation between the lid and the gate movements is not, however, observed in the NMR structure.

PubMed: 22297982
DOI: 10.1107/S1744309111052341

実験手法

X-RAY DIFFRACTION (2.5 Å)