Literature DB >> 23027753

Crystallization and preliminary diffraction studies of GIM-1, a class B carbapenem-hydrolyzing β-lactamase.

Myoung-Ki Hong1, Jung Hun Lee, Dae Beom Kwon, Jin-Kwang Kim, Thi-Huyen Tran, Dinh-Duc Nguyen, Byeong Chul Jeong, Sang Hee Lee, Lin-Woo Kang.   

Abstract

GIM-1 is a member of the class B carbapenemases (metallo-β-lactamases; MBLs) and has a wide spectrum of activity against carbapenems, penicillins and extended-spectrum cephalosporins, but not aztreonam. GIM-1 presents an enormous challenge to infection control, particularly in the eradication of Gram-negative pathogens including Enterobacteriaceae, Pseudomonas aeruginosa, Acinetobacter baumannii and nonfermenters. There are presently few or no drugs in late-stage development for these pathogens and GIM-1 is a potential target for the development of antimicrobial agents against pathogens producing MBLs. In this study, GIM-1 was cloned, overexpressed and crystallized. The GIM-1 crystals diffracted to 1.4 Å resolution and belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 38.5, b = 67.6, c = 72.8 Å. One molecule is present in the asymmetric unit, with a corresponding V(M) of 1.69 Å(3) Da(-1) and a solvent content of 27.1%.

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Year:  2012        PMID: 23027753      PMCID: PMC3497985          DOI: 10.1107/S1744309112035695

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN: 1744-3091


  15 in total

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Review 1.  Structural basis for carbapenem-hydrolyzing mechanisms of carbapenemases conferring antibiotic resistance.

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2.  Detection of blaOXA-145, blaOXA-224, blaOXA-539, and blaOXA-675 Genes and Carbapenem-Hydrolyzing Class D β-Lactamases (CHDLs) in Clinical Isolates of Pseudomonas aeruginosa Collected from West of Iran, Hamadan.

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