View source for 7x4l


==Crystal structure of Bacteroides thetaiotaomicron glutamate decarboxylase mutant Y303F-PLP complex==
<StructureSection load='7x4l' size='340' side='right'caption='[[7x4l]], [[Resolution|resolution]] 2.59&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7x4l]] is a 6 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=7X4L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7X4L 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]] 2.59&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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=7x4l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7x4l OCA], [https://pdbe.org/7x4l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7x4l RCSB], [https://www.ebi.ac.uk/pdbsum/7x4l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7x4l ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8A4M9_BACTN Q8A4M9_BACTN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Glutamate decarboxylase catalyzes the conversion of glutamate to gamma-aminobutyric acid, which plays a vital role in the gut-brain axis. Herein, a novel glutamate decarboxylase from Bacteroides thetaiotaomicron (BTGAD) was heterologously expressed. BTGAD possessed high catalytic efficiency at 60â and pH 3.6. As pH response, N-terminal sequence (NTS), C-terminal sequence (CTS), and beta-hairpin in BTGAD coordinately regulated its activity under different pH. NTS folded into a loop under acidic pH, and the truncation of NTS severely reduced its activity to 4.2%. While CTS occupied the active site under neutral pH and became disordered to release the inhibition effect under acidic conditions. The beta-hairpin, located near the active site, swung and formed open and closed conformations, which acted as an activity switch. This study provides the molecular basis for the coordinated regulation mechanism of BTGAD and lays a theoretical foundation for understanding the metabolism of dietary glutamate and its interaction relationships with the gut-brain axis.

Coordinated regulation of Bacteroides thetaiotaomicron glutamate decarboxylase activity by multiple elements under different pH.,Liu S, Wen B, Du G, Wang Y, Ma X, Yu H, Zhang J, Fan S, Zhou H, Xin F Food Chem. 2023 Mar 1;403:134436. doi: 10.1016/j.foodchem.2022.134436. Epub 2022 , Sep 28. PMID:36358099<ref>PMID:36358099</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7x4l" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacteroides thetaiotaomicron VPI-5482]]
[[Category: Large Structures]]
[[Category: Boting W]]
[[Category: Guoming D]]
[[Category: Liu S]]
[[Category: Xin F]]
[[Category: Yulu W]]