6N14

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

Summary for 6N14

• Entry DOI: 10.2210/pdb6n14/pdb
• Descriptor: Beta-lactamase, PHOSPHATE ION (3 entities in total)
• Functional Keywords: phosphoserine, beta-lactamase, mycobacterium tuberculosis, inhibitor, hydrolase
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 1
• Total formula weight: 32889.73

Authors

Moural, T.W.,White, D.S.,Choy, C.J.,Kang, C.,Berkman, C.E. (deposition date: 2018-11-08, release date: 2019-08-28, Last modification date: 2024-11-13)

Primary citation

Moural, T.W.,White, D.S.,Choy, C.J.,Kang, C.,Berkman, C.E.
Crystal Structure of Phosphoserine BlaC fromMycobacterium tuberculosisInactivated by Bis(Benzoyl) Phosphate.
Int J Mol Sci, 20:-, 2019

PubMed Abstract: , the pathogen responsible for tuberculosis (TB), is the leading cause of death from infectious disease worldwide. The class A serine β-lactamase BlaC confers resistance to conventional β-lactam antibiotics. As the primary mechanism of bacterial resistance to β-lactam antibiotics, the expression of a β-lactamase by results in hydrolysis of the β-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 β-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.

PubMed: 31269656
DOI: 10.3390/ijms20133247

Experimental method

X-RAY DIFFRACTION (1.52169460473 Å)