7XRV

Bacteroides thetaiotaomicron ferulic acid esterase - S150A (BT_4077-S150A) complex with trans-methylferulate

Summary for 7XRV

• Entry DOI: 10.2210/pdb7xrv/pdb
• Related: 7XRT
• Descriptor: Ferulic acid esterase, CALCIUM ION, Trans-methylferulate, ... (4 entities in total)
• Functional Keywords: esterase, complex, hydrolase
• Biological source: Bacteroides thetaiotaomicron VPI-5482
• Total number of polymer chains: 10
• Total formula weight: 335096.54

Authors

Du, G.M.,Wang, Y.L.,Xin, F.J. (deposition date: 2022-05-11, release date: 2023-11-22, Last modification date: 2024-11-06)

Primary citation

Wang, Y.,Du, G.,Zhang, Y.,Yu, H.,Liu, S.,Wang, Z.,Ma, X.,Wei, X.,Wen, B.,Li, Z.,Fan, S.,Xin, F.
Distinct Adjacent Substrate Binding Pocket Regulates the Activity of a Decameric Feruloyl Esterase from Bacteroides thetaiotaomicron.
J.Agric.Food Chem., 72:23554-23566, 2024

PubMed Abstract: Understanding how the human gut microbiota contribute to the metabolism of dietary carbohydrates is of great interest, particularly those with ferulic acid (FA) decorations that have manifold health benefits. Here, we report the crystal structure of a decameric feruloyl esterase (Fae) from in complex with methyl ferulate (MFA), revealing that MFA is situated in a noncatalytic substrate binding pocket adjacent to the catalytic pocket. Molecular docking and mutagenesis studies further demonstrated that the adjacent pocket affects substrate binding in the active site and negatively regulates the Fae activity on both synthetic and natural xylan substrates. Additionally, quantum mechanics (QM) calculations were employed to investigate the catalytic process of Fae from substrate binding to product release, and identified TS_2 in the acylation step is rate-limiting. Collectively, this study unmasks a novel regulatory mechanism of FAE activity, which may contribute to further investigation of FA-conjugated polysaccharides metabolism in the human gut.

PubMed: 39370616
DOI: 10.1021/acs.jafc.4c06286

Experimental method

X-RAY DIFFRACTION (2.713 Å)