5nj2

Crystal structure of BlaC from Mycobacterium tuberculosis bound to phosphate

spinqualitylabelsall models 5nj2, resolution 1.19Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5nj2 is a 2 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 1.19Å Ligands: ACT, AE4, ETE, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function BLAC_MYCTU Publication Abstract from PubMed The rise of multi- and even totally antibiotic resistant forms of Mycobacterium tuberculosis underlines the need for new antibiotics. The pathogen is resistant to beta-lactam compounds due to its native serine beta-lactamase, BlaC. This resistance can be circumvented by administration of a beta-lactamase inhibitor. We studied the interaction between BlaC and the inhibitor clavulanic acid. Our data show hydrolysis of clavulanic acid and recovery of BlaC activity upon prolonged incubation. The rate of clavulanic acid hydrolysis is much higher in the presence of phosphate ions. A specific binding site for phosphate is identified in the active site pocket, both in the crystalline state and in solution. NMR spectroscopy experiments show that phosphate binds to this site with a dissociation constant of 30 mM in the free enzyme. We conclude that inhibition of BlaC by clavulanic acid is reversible and that phosphate ions can promote the hydrolysis of the inhibitor. Phosphate Promotes the Recovery of Mycobacterium tuberculosis beta-Lactamase from Clavulanic Acid Inhibition.,Elings W, Tassoni R, van der Schoot SA, Luu W, Kynast JP, Dai L, Blok AJ, Timmer M, Florea BI, Pannu NS, Ubbink M Biochemistry. 2017 Nov 14. doi: 10.1021/acs.biochem.7b00556. PMID:29087696 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta-lactamase 3D structures

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