6xpp

Crystal structure of itaconate modified Mycobaterium tuberculosis isocitrate lyase

spinqualitylabelsall models 6xpp, resolution 1.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6xpp is a 4 chain structure with sequence from Mycobacterium tuberculosis H37Rv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.55Å Ligands: ITN, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ACEA_MYCTU Catalyzes the formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle. May be involved in the assimilation of one-carbon compounds via the isocitrate lyase-positive serine pathway (By similarity). Publication Abstract from PubMed Itaconate is a mammalian antimicrobial metabolite that inhibits the isocitrate lyases (ICLs) of Mycobacterium tuberculosis. Herein, we report that ICLs form a covalent adduct with itaconate through their catalytic cysteine residue. These results reveal atomic details of itaconate inhibition and provide insights into the catalytic mechanism of ICLs. Itaconate is a covalent inhibitor of the Mycobacterium tuberculosis isocitrate lyase.,Kwai BXC, Collins AJ, Middleditch MJ, Sperry J, Bashiri G, Leung IKH RSC Med Chem. 2020 Oct 19;12(1):57-61. doi: 10.1039/d0md00301h. eCollection 2021 , Jan 1. PMID:34046597 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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