9t6a | pdb_00009t6a

Glutamate decarboxylase from Mycobacterium tuberculosis at 1.41 A resolution.

spinqualitylabelsall models 9t6a, resolution 1.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9t6a is a 1 chain structure with sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.25Å Ligands: ACT, LLP, PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function O06249_MYCTO 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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