6n14 | pdb_00006n14

Phosphoserine BlaC, Class A serine beta-lactamase from Mycobacterium tuberculosis

spinqualitylabelsall models 6n14, resolution 1.52Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6n14 is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PO4 NonStd Res: SEP Activity: Beta-lactamase, with EC number 3.5.2.6 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Mycobacterium tuberculosis, the pathogen responsible for tuberculosis (TB), is the leading cause of death from infectious disease worldwide. The class A serine beta-lactamase BlaC confers Mycobacterium tuberculosis resistance to conventional beta-lactam antibiotics. As the primary mechanism of bacterial resistance to beta-lactam antibiotics, the expression of a beta-lactamase by Mycobacterium tuberculosis results in hydrolysis of the beta-lactam ring and deactivation of these antibiotics. In this study, we conducted protein X-ray crystallographic analysis of the inactivation of BlaC, upon exposure to the inhibitor bis(benzoyl) phosphate. Crystal structure data confirms that serine beta-lactamase is phosphorylated at the catalytic serine residue (Ser-70) by this phosphate-based inactivator. This new crystallographic evidence suggests a mechanism for phosphorylation of BlaC inhibition by bis(benzoyl) phosphate over acylation. Additionally, we confirmed that bis(benzoyl) phosphate inactivated BlaC in a time-dependent manner. Crystal Structure of Phosphoserine BlaC from Mycobacterium tuberculosis Inactivated by Bis(Benzoyl) Phosphate.,Moural TW, White DS, Choy CJ, Kang C, Berkman CE Int J Mol Sci. 2019 Jul 2;20(13). pii: ijms20133247. doi: 10.3390/ijms20133247. PMID:31269656 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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