7DQ9

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

Summary for 7DQ9

• Entry DOI: 10.2210/pdb7dq9/pdb
• Descriptor: Predicted hydrolases or acyltransferases (Alpha/beta hydrolase superfamily) (2 entities in total)
• Functional Keywords: gut microorganisms, alistipes shahii, esterase, ester bond, hydrolase
• Biological source: Alistipes shahii WAL 8301
• Total number of polymer chains: 4
• Total formula weight: 118168.06

Authors

Wei, X.,Gu, T.Y.,Xin, F.J.,Wang, Y.L. (deposition date: 2020-12-22, release date: 2021-12-22, Last modification date: 2023-11-29)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.702 Å)