6T5O

Bacteroides salyersiae GH164 beta-mannosidase

これはPDB形式変換不可エントリーです。

6T5O の概要

• エントリーDOI: 10.2210/pdb6t5o/pdb
• 分子名称: Glyco_hydro_42M domain-containing protein, 1,2-ETHANEDIOL, S,R MESO-TARTARIC ACID, ... (8 entities in total)
• 機能のキーワード: beta-mannosidase glycoside hydrolase, hydrolase
• 由来する生物種: Bacteroides salyersiae
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 462981.27

構造登録者

Armstrong, Z.,Davies, G. (登録日: 2019-10-16, 公開日: 2020-01-01, 最終更新日: 2024-05-15)

主引用文献

Armstrong, Z.,Davies, G.J.
Structure and function ofBs164 beta-mannosidase fromBacteroides salyersiaethe founding member of glycoside hydrolase family GH164.
J.Biol.Chem., 295:4316-4326, 2020

PubMed Abstract: Recent work exploring protein sequence space has revealed a new glycoside hydrolase (GH) family (GH164) of putative mannosidases. GH164 genes are present in several commensal bacteria, implicating these genes in the degradation of dietary glycans. However, little is known about the structure, mechanism of action, and substrate specificity of these enzymes. Herein we report the biochemical characterization and crystal structures of the founding member of this family (164) from the human gut symbiont Previous reports of this enzyme indicated that it has α-mannosidase activity, however, we conclusively show that it cleaves only β-mannose linkages. Using NMR spectroscopy, detailed enzyme kinetics of WT and mutant 164, and multiangle light scattering we found that it is a trimeric retaining β-mannosidase, that is susceptible to several known mannosidase inhibitors. X-ray crystallography revealed the structure of 164, the first known structure of a GH164, at 1.91 Å resolution. 164 is composed of three domains: a (β/α) barrel, a trimerization domain, and a β-sandwich domain, representing a previously unobserved structural-fold for β-mannosidases. Structures of 164 at 1.80-2.55 Å resolution in complex with the inhibitors noeuromycin, mannoimidazole, or 2,4-dinitrophenol 2-deoxy-2-fluoro-mannoside reveal the residues essential for specificity and catalysis including the catalytic nucleophile (Glu-297) and acid/base residue (Glu-160). These findings further our knowledge of the mechanisms commensal microbes use for nutrient acquisition.

PubMed: 31871050
DOI: 10.1074/jbc.RA119.011591

実験手法

X-RAY DIFFRACTION (1.91 Å)