6Z2D

Crystal structure of wild type OgpA from Akkermansia muciniphila in P 41 21 2

6Z2D の概要

• エントリーDOI: 10.2210/pdb6z2d/pdb
• 分子名称: O-glycan protease, TETRAETHYLENE GLYCOL, 1,2-ETHANEDIOL, ... (6 entities in total)
• 機能のキーワード: o-glycan endopeptidase, mucins, ogpa. metalloprotease, hydrolase
• 由来する生物種: Akkermansia muciniphila ATCC BAA-835
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 42344.28

構造登録者

Trastoy, B.,Naegali, A.,Anso, I.,Sjogren, J.,Guerin, M.E. (登録日: 2020-05-15, 公開日: 2020-09-30, 最終更新日: 2024-06-19)

主引用文献

Trastoy, B.,Naegeli, A.,Anso, I.,Sjogren, J.,Guerin, M.E.
Structural basis of mammalian mucin processing by the human gut O-glycopeptidase OgpA from Akkermansia muciniphila.
Nat Commun, 11:4844-4844, 2020

PubMed Abstract: Akkermansia muciniphila is a mucin-degrading bacterium commonly found in the human gut that promotes a beneficial effect on health, likely based on the regulation of mucus thickness and gut barrier integrity, but also on the modulation of the immune system. In this work, we focus in OgpA from A. muciniphila, an O-glycopeptidase that exclusively hydrolyzes the peptide bond N-terminal to serine or threonine residues substituted with an O-glycan. We determine the high-resolution X-ray crystal structures of the unliganded form of OgpA, the complex with the glycodrosocin O-glycopeptide substrate and its product, providing a comprehensive set of snapshots of the enzyme along the catalytic cycle. In combination with O-glycopeptide chemistry, enzyme kinetics, and computational methods we unveil the molecular mechanism of O-glycan recognition and specificity for OgpA. The data also contribute to understanding how A. muciniphila processes mucins in the gut, as well as analysis of post-translational O-glycosylation events in proteins.

PubMed: 32973204
DOI: 10.1038/s41467-020-18696-y

実験手法

X-RAY DIFFRACTION (1.899 Å)