7EBP

The structural analysis of A.Muciniphila sulfatase

7EBP の概要

• エントリーDOI: 10.2210/pdb7ebp/pdb
• 分子名称: Sulfatase, CALCIUM ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: akkermansia muciniphila sulfatase mucin, hydrolase
• 由来する生物種: Akkermansia muciniphila ATCC BAA-835
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 121719.84

構造登録者

Bao, R.,Li, C.C.,Tang, X.Y.,Zhu, Y.B.,Song, Y.J.,Zhao, N.L.,Huang, Q.,Mou, X.Y.,Luo, G.H.,Liu, T.G. (登録日: 2021-03-10, 公開日: 2022-03-30, 最終更新日: 2023-11-29)

主引用文献

Li, C.C.,Tang, X.Y.,Zhu, Y.B.,Song, Y.J.,Zhao, N.L.,Huang, Q.,Mou, X.Y.,Luo, G.H.,Liu, T.G.,Tong, A.P.,Tang, H.,Bao, R.
Structural analysis of the sulfatase AmAS from Akkermansia muciniphila.
Acta Crystallogr D Struct Biol, 77:1614-1623, 2021

PubMed Abstract: Akkermansia muciniphila, an anaerobic Gram-negative bacterium, is a major intestinal commensal bacterium that can modulate the host immune response. It colonizes the mucosal layer and produces nutrients for the gut mucosa and other commensal bacteria. It is believed that mucin desulfation is the rate-limiting step in the mucin-degradation process, and bacterial sulfatases that carry out mucin desulfation have been well studied. However, little is known about the structural characteristics of A. muciniphila sulfatases. Here, the crystal structure of the premature form of the A. muciniphila sulfatase AmAS was determined. Structural analysis combined with docking experiments defined the critical active-site residues that are responsible for catalysis. The loop regions I-V were proposed to be essential for substrate binding. Structure-based sequence alignment and structural superposition allow further elucidation of how different subclasses of formylglycine-dependent sulfatases (FGly sulfatases) adopt the same catalytic mechanism but exhibit diverse substrate specificities. These results advance the understanding of the substrate-recognition mechanisms of A. muciniphila FGly-type sulfatases. Structural variations around the active sites account for the different substrate-binding properties. These results will enhance the understanding of the roles of bacterial sulfatases in the metabolism of glycans and host-microbe interactions in the human gut environment.

PubMed: 34866616
DOI: 10.1107/S2059798321010317

実験手法

X-RAY DIFFRACTION (1.80000050381 Å)