6FXP

Crystal structure of S. aureus glucosaminidase B

6FXP の概要

• エントリーDOI: 10.2210/pdb6fxp/pdb
• 分子名称: Uncharacterized protein, TETRAETHYLENE GLYCOL, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: lysozyme-like fold, n-acetylglucosaminidase, peptidoglycan hydrolase, gh73, hydrolase
• 由来する生物種: Staphylococcus aureus subsp. aureus Mu50
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 59647.03

構造登録者

Pintar, S.,Turk, D. (登録日: 2018-03-09, 公開日: 2019-03-20, 最終更新日: 2024-05-08)

主引用文献

Pintar, S.,Borisek, J.,Usenik, A.,Perdih, A.,Turk, D.
Domain sliding of two Staphylococcus aureus N-acetylglucosaminidases enables their substrate-binding prior to its catalysis.
Commun Biol, 3:178-178, 2020

PubMed Abstract: To achieve productive binding, enzymes and substrates must align their geometries to complement each other along an entire substrate binding site, which may require enzyme flexibility. In pursuit of novel drug targets for the human pathogen S. aureus, we studied peptidoglycan N-acetylglucosaminidases, whose structures are composed of two domains forming a V-shaped active site cleft. Combined insights from crystal structures supported by site-directed mutagenesis, modeling, and molecular dynamics enabled us to elucidate the substrate binding mechanism of SagB and AtlA-gl. This mechanism requires domain sliding from the open form observed in their crystal structures, leading to polysaccharide substrate binding in the closed form, which can enzymatically process the bound substrate. We suggest that these two hydrolases must exhibit unusual extents of flexibility to cleave the rigid structure of a bacterial cell wall.

PubMed: 32313083
DOI: 10.1038/s42003-020-0911-7

実験手法

X-RAY DIFFRACTION (2.03 Å)