View source for 7xrv


==Bacteroides thetaiotaomicron ferulic acid esterase - S150A (BT_4077-S150A) complex with trans-methylferulate==
<StructureSection load='7xrv' size='340' side='right'caption='[[7xrv]], [[Resolution|resolution]] 2.71&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7xrv]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_thetaiotaomicron_VPI-5482 Bacteroides thetaiotaomicron VPI-5482]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XRV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XRV FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.713&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SZQ:methyl+(~{E})-3-(3-methoxy-4-oxidanyl-phenyl)prop-2-enoate'>SZQ</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7xrv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xrv OCA], [https://pdbe.org/7xrv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xrv RCSB], [https://www.ebi.ac.uk/pdbsum/7xrv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xrv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8A0E4_BACTN Q8A0E4_BACTN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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 (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<ref>PMID:39370616</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7xrv" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacteroides thetaiotaomicron VPI-5482]]
[[Category: Large Structures]]
[[Category: Du GM]]
[[Category: Wang YL]]
[[Category: Xin FJ]]