6Z2D

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

Summary for 6Z2D

• Entry DOI: 10.2210/pdb6z2d/pdb
• Descriptor: O-glycan protease, TETRAETHYLENE GLYCOL, 1,2-ETHANEDIOL, ... (6 entities in total)
• Functional Keywords: o-glycan endopeptidase, mucins, ogpa. metalloprotease, hydrolase
• Biological source: Akkermansia muciniphila ATCC BAA-835
• Total number of polymer chains: 1
• Total formula weight: 42344.28

Authors

Trastoy, B.,Naegali, A.,Anso, I.,Sjogren, J.,Guerin, M.E. (deposition date: 2020-05-15, release date: 2020-09-30, Last modification date: 2024-06-19)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.899 Å)