Structural highlights
FunctionPublication Abstract from PubMedUnderstanding 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 (BtFae) from Bacteroides thetaiotaomicron 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 BtFae activity on both synthetic and natural xylan substrates. Additionally, quantum mechanics (QM) calculations were employed to investigate the catalytic process of BtFae 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. Distinct Adjacent Substrate Binding Pocket Regulates the Activity of a Decameric Feruloyl Esterase from Bacteroides thetaiotaomicron.,Wang Y, Du G, Zhang Y, Yu H, Liu S, Wang Z, Ma X, Wei X, Wen B, Li Z, Fan S, Xin F J Agric Food Chem. 2024 Oct 23;72(42):23554-23566. doi: 10.1021/acs.jafc.4c06286. , Epub 2024 Oct 6. PMID:39370616[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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