7OZC

Sulfated host glycan recognition by carbohydrate sulfatases of the human gut microbiota (BT3109_S1_15)

これはPDB形式変換不可エントリーです。

7OZC の概要

• エントリーDOI: 10.2210/pdb7ozc/pdb
• 分子名称: Arylsulfatase A, 6-O-sulfo-beta-D-galactopyranose, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: host glycans, sulfation, carbohydrate sulfatases, microbiota, hydrolase
• 由来する生物種: Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 57441.60

構造登録者

Cartmell, A. (登録日: 2021-06-27, 公開日: 2022-06-29, 最終更新日: 2024-01-31)

主引用文献

Luis, A.S.,Basle, A.,Byrne, D.P.,Wright, G.S.A.,London, J.A.,Jin, C.,Karlsson, N.G.,Hansson, G.C.,Eyers, P.A.,Czjzek, M.,Barbeyron, T.,Yates, E.A.,Martens, E.C.,Cartmell, A.
Sulfated glycan recognition by carbohydrate sulfatases of the human gut microbiota.
Nat.Chem.Biol., 18:841-849, 2022

PubMed Abstract: Sulfated glycans are ubiquitous nutrient sources for microbial communities that have coevolved with eukaryotic hosts. Bacteria metabolize sulfated glycans by deploying carbohydrate sulfatases that remove sulfate esters. Despite the biological importance of sulfatases, the mechanisms underlying their ability to recognize their glycan substrate remain poorly understood. Here, we use structural biology to determine how sulfatases from the human gut microbiota recognize sulfated glycans. We reveal seven new carbohydrate sulfatase structures spanning four S1 sulfatase subfamilies. Structures of S1_16 and S1_46 represent novel structures of these subfamilies. Structures of S1_11 and S1_15 demonstrate how non-conserved regions of the protein drive specificity toward related but distinct glycan targets. Collectively, these data reveal that carbohydrate sulfatases are highly selective for the glycan component of their substrate. These data provide new approaches for probing sulfated glycan metabolism while revealing the roles carbohydrate sulfatases play in host glycan catabolism.

PubMed: 35710619
DOI: 10.1038/s41589-022-01039-x

実験手法

X-RAY DIFFRACTION (1.75 Å)