4K40

Peptidoglycan O-acetylesterase in action, 0 min

4K40 の概要

• エントリーDOI: 10.2210/pdb4k40/pdb
• 関連するPDBエントリー: 4K3U
• 分子名称: GDSL-like Lipase/Acylhydrolase family protein (2 entities in total)
• 機能のキーワード: alpha/beta fold, peptidoglycan hydrolase, hydrolase
• 由来する生物種: Neisseria meningitidis LNP21362
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 81581.58

構造登録者

Williams, A.H.,Gompert Boneca, I. (登録日: 2013-04-11, 公開日: 2014-09-03, 最終更新日: 2024-10-30)

主引用文献

Williams, A.H.,Veyrier, F.J.,Bonis, M.,Michaud, Y.,Raynal, B.,Taha, M.K.,White, S.W.,Haouz, A.,Boneca, I.G.
Visualization of a substrate-induced productive conformation of the catalytic triad of the Neisseria meningitidis peptidoglycan O-acetylesterase reveals mechanistic conservation in SGNH esterase family members.
Acta Crystallogr.,Sect.D, 70:2631-2639, 2014

PubMed Abstract: Peptidoglycan O-acetylesterase (Ape1), which is required for host survival in Neisseria sp., belongs to the diverse SGNH hydrolase superfamily, which includes important viral and bacterial virulence factors. Here, multi-domain crystal structures of Ape1 with an SGNH catalytic domain and a newly identified putative peptidoglycan-detection module are reported. Enzyme catalysis was performed in Ape1 crystals and key catalytic intermediates along the SGNH esterase hydrolysis reaction pathway were visualized, revealing a substrate-induced productive conformation of the catalytic triad, a mechanistic detail that has not previously been observed. This substrate-induced productive conformation of the catalytic triad shifts the established dogma on these enzymes, generating valuable insight into the structure-based design of drugs targeting the SGNH esterase superfamily.

PubMed: 25286847
DOI: 10.1107/S1399004714016770

実験手法

X-RAY DIFFRACTION (2.634 Å)