8IOX

Escherichia coli OpgD mutant-D388N

8IOX の概要

• エントリーDOI: 10.2210/pdb8iox/pdb
• 分子名称: Glucans biosynthesis protein D, alpha-D-glucopyranose-(1-1)-alpha-D-glucopyranose (3 entities in total)
• 機能のキーワード: beta-1, 2-glucanase, hydrolase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 770222.36

構造登録者

Motouchi, S.,Nakajima, M. (登録日: 2023-03-13, 公開日: 2024-03-13, 最終更新日: 2024-10-16)

主引用文献

Motouchi, S.,Kobayashi, K.,Nakai, H.,Nakajima, M.
Identification of enzymatic functions of osmo-regulated periplasmic glucan biosynthesis proteins from Escherichia coli reveals a novel glycoside hydrolase family.
Commun Biol, 6:961-961, 2023

PubMed Abstract: Most Gram-negative bacteria synthesize osmo-regulated periplasmic glucans (OPG) in the periplasm or extracellular space. Pathogenicity of many pathogens is lost by knocking out opgG, an OPG-related gene indispensable for OPG synthesis. However, the biochemical functions of OpgG and OpgD, a paralog of OpgG, have not been elucidated. In this study, structural and functional analyses of OpgG and OpgD from Escherichia coli revealed that these proteins are β-1,2-glucanases with remarkably different activity from each other, establishing a new glycoside hydrolase family, GH186. Furthermore, a reaction mechanism with an unprecedentedly long proton transfer pathway among glycoside hydrolase families is proposed for OpgD. The conformation of the region that forms the reaction pathway differs noticeably between OpgG and OpgD, which explains the observed low activity of OpgG. The findings enhance our understanding of OPG biosynthesis and provide insights into functional diversity for this novel enzyme family.

PubMed: 37735577
DOI: 10.1038/s42003-023-05336-6

実験手法

X-RAY DIFFRACTION (2.95 Å)