7DQ9

Crystal structure of a type-A feruloyl esterase from gut Alistipes shahii

7DQ9 の概要

• エントリーDOI: 10.2210/pdb7dq9/pdb
• 分子名称: Predicted hydrolases or acyltransferases (Alpha/beta hydrolase superfamily) (2 entities in total)
• 機能のキーワード: gut microorganisms, alistipes shahii, esterase, ester bond, hydrolase
• 由来する生物種: Alistipes shahii WAL 8301
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 118168.06

構造登録者

Wei, X.,Gu, T.Y.,Xin, F.J.,Wang, Y.L. (登録日: 2020-12-22, 公開日: 2021-12-22, 最終更新日: 2023-11-29)

主引用文献

Wei, X.,Wang, Y.L.,Wen, B.T.,Liu, S.J.,Wang, L.,Sun, L.,Gu, T.Y.,Li, Z.,Bao, Y.,Fan, S.L.,Zhou, H.,Wang, F.,Xin, F.
The alpha-Helical Cap Domain of a Novel Esterase from Gut Alistipes shahii Shaping the Substrate-Binding Pocket.
J.Agric.Food Chem., 69:6064-6072, 2021

PubMed Abstract: The human gut microbiota regulates nutritional metabolism, especially by encoding specific ferulic acid esterases (FAEs) to release functional ferulic acid (FA) from dietary fiber. In our previous study, we observed seven upregulated FAE genes during fecal slurry fermentation using wheat bran. Here, a 29 kDa FAE (FAE) from of was characterized and identified as the type-A FAE. The X-ray structure of FAE has been determined, revealing a unique α-helical domain comprising five α-helices, which was first characterized in FAEs from the gut microbiota. Further molecular docking analysis and biochemical studies revealed that Tyr100, Thr122, Tyr219, and Ile220 are essential for substrate binding and catalytic efficiency. Additionally, Glu129 and Lys130 in the cap domain shaped the substrate-binding pocket and affected the substrate preference. This is the first report on FAE, providing a theoretical basis for the dietary metabolism in the human gut.

PubMed: 33979121
DOI: 10.1021/acs.jafc.1c00940

実験手法

X-RAY DIFFRACTION (1.702 Å)