4PMQ

Crystal structure of the Mycobacterium tuberculosis Tat-secreted protein Rv2525c in complex with L-tartrate (orthorhombic crystal form)

4PMQ の概要

• エントリーDOI: 10.2210/pdb4pmq/pdb
• 分子名称: Tat-secreted protein Rv2525c, L(+)-TARTARIC ACID, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: unknown function
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22585.91

構造登録者

Bellinzoni, M.,Haouz, A.,Shepard, W.,Alzari, P.M. (登録日: 2014-05-22, 公開日: 2014-10-08, 最終更新日: 2023-12-20)

主引用文献

Bellinzoni, M.,Haouz, A.,Miras, I.,Magnet, S.,Andre-Leroux, G.,Mukherjee, R.,Shepard, W.,Cole, S.T.,Alzari, P.M.
Structural studies suggest a peptidoglycan hydrolase function for the Mycobacterium tuberculosis Tat-secreted protein Rv2525c.
J.Struct.Biol., 188:156-164, 2014

PubMed Abstract: Among the few proteins shown to be secreted by the Tat system in Mycobacterium tuberculosis, Rv2525c is of particular interest, since its gene is conserved in the minimal genome of Mycobacterium leprae. Previous evidence linked this protein to cell wall metabolism and sensitivity to β-lactams. We describe here the crystal structure of Rv2525c that shows a TIM barrel-like fold characteristic of glycoside hydrolases of the GH25 family, which includes prokaryotic and phage-encoded peptidoglycan hydrolases. Structural comparison with other members of this family combined with substrate docking suggest that, although the 'neighbouring group' catalytic mechanism proposed for this family still appears as the most plausible, the identity of residues involved in catalysis in GH25 hydrolases might need to be revised.

PubMed: 25260828
DOI: 10.1016/j.jsb.2014.09.003

実験手法

X-RAY DIFFRACTION (1.61 Å)