9t6a: Difference between revisions
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==Glutamate decarboxylase from Mycobacterium tuberculosis at 1.41 A resolution.== | |||
<StructureSection load='9t6a' size='340' side='right'caption='[[9t6a]], [[Resolution|resolution]] 1.25Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9t6a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9T6A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9T6A 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]] 1.25Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=9t6a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9t6a OCA], [https://pdbe.org/9t6a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9t6a RCSB], [https://www.ebi.ac.uk/pdbsum/9t6a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9t6a ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/O06249_MYCTO O06249_MYCTO] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Glutamate decarboxylase (GadB) is a pyridoxal phosphate (PLP)-dependent enzyme that contributes to intracellular pH homeostasis and supports the survival of Mycobacterium tuberculosis (Mtb) in lung tissue, granulomas, and within host macrophages. Here, we demonstrate that glutamate decarboxylase from Mycobacterium tuberculosis (MtbGadB) is a multimeric enzyme exhibiting maximal activity under acidic conditions. MtbGadB is inhibited by the clinical antibiotic d-cycloserine as well as l-cycloserine in vitro. Both cycloserine enantiomers break the internal aldimine bond between PLP and the conserved Lys277 residue, forming a previously unrecognised PLP-oxime product and subsequently inhibiting catalysis. Given that PLP-dependent enzymes are promising drug targets, understanding the chemical behaviour of PLP is essential for developing selective inhibitors. | |||
Cycloserine inhibits glutamate decarboxylase from Mycobacterium tuberculosis.,Snasel J, Dostal J, Tupec M, Bulvas O, Pichova I J Enzyme Inhib Med Chem. 2026 Dec;41(1):2707854. doi: , 10.1080/14756366.2026.2707854. Epub 2026 Sep 21. PMID:42765272<ref>PMID:42765272</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 9t6a" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mycobacterium tuberculosis]] | |||
[[Category: Dostal J]] | |||
[[Category: Pichova I]] | |||
[[Category: Snasel J]] | |||
Latest revision as of 09:36, 30 September 2026
Glutamate decarboxylase from Mycobacterium tuberculosis at 1.41 A resolution.
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