6JV4

Crystal structure of metallo-beta-lactamase VMB-1

Summary for 6JV4

• Entry DOI: 10.2210/pdb6jv4/pdb
• Descriptor: VMB-1, ZINC ION, CITRIC ACID, ... (4 entities in total)
• Functional Keywords: metallo-beta-lactamase, subclasse b1, hydrolase
• Biological source: Vibrio alginolyticus
• Total number of polymer chains: 4
• Total formula weight: 104112.48

Authors

Cheng, Q.,Chen, S. (deposition date: 2019-04-15, release date: 2019-11-27, Last modification date: 2024-03-27)

Primary citation

Zheng, Z.,Cheng, Q.,Chan, E.W.,Chen, S.
Genetic and Biochemical Characterization of VMB-1, a Novel Metallo-beta-Lactamase Encoded by a Conjugative, Broad-Host Range IncC Plasmid from Vibrio spp.
Adv Biosyst, 4:e1900221-e1900221, 2020

PubMed Abstract: The increasing incidence of phenotypic resistance to carbapenems in recent years is mainly attributed to acquisition of mobile carbapenemase-encoding genetic elements by major bacterial pathogens. Here, a novel carbapenemase known as Vibrio metallo-β-lactamase 1 (VMB-1), which is encoded by a gene (bla ) located in an integron-bearing, highly transmissible IncC type plasmid, namely pVB1796, is identified and characterized, both genetically and functionally. Recovered from a foodborne Vibrio alginolyticus strain that exhibits resistance to all known β-lactam antibiotics, pVB1796 is found to possess a hybrid backbone that exhibits unique features of both type 1 and type 2 IncC elements. VMB-1 exhibits 94% sequence homology with several recently reported but poorly characterized metallo-β-lactamases (MBLs) produced by the marine organisms Alteromonadaceae, Glaciecola, and Thalassomonas actiniarum. Sequence alignment analysis shows that VMB-1 shares a structurally identical active site with subclass B1 MBLs. Importantly, pVB1796 is found to be efficiently transferred from Vibrio to other Gram-negative bacterial pathogens, including Salmonella typhimurium, Klebsiella pneumoniae, and Acinetobacter baumanni, via conjugation. These findings suggest that bla -bearing plasmids have the potential to be disseminated to other Gram-negative bacterial pathogens in the near future and render carbapenems useless in treatment of multidrug resistant infections.

PubMed: 32293144
DOI: 10.1002/adbi.201900221

Experimental method

X-RAY DIFFRACTION (1.7 Å)