1KO3

VIM-2, a Zn-beta-lactamase from Pseudomonas aeruginosa with Cys221 reduced

Summary for 1KO3

• Entry DOI: 10.2210/pdb1ko3/pdb
• Related: 1KO2
• Descriptor: VIM-2 metallo-beta-lactamase, ZINC ION, ACETATE ION, ... (6 entities in total)
• Functional Keywords: alpha-beta/beta-alpha fold, hydrolase
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 1
• Total formula weight: 24889.02

Authors

Garcia-Saez, I.,Docquier, J.-D.,Rossolini, G.M.,Dideberg, O. (deposition date: 2001-12-20, release date: 2003-09-02, Last modification date: 2023-10-25)

Primary citation

Garcia-Saez, I.,Docquier, J.-D.,Rossolini, G.M.,Dideberg, O.
The three-dimensional structure of VIM-2, a Zn-beta-lactamase from Pseudomonas aeruginosa in its reduced and oxidised form
J.Mol.Biol., 375:604-611, 2008

PubMed Abstract: The crystal structures of the universally widespread metallo-beta-lactamase (MBL) Verona integron-encoded MBL (VIM)-2 from Pseudomonas aeruginosa have been solved in their native form as well as in an unexpected oxidised form. This carbapenem-hydrolysing enzyme belongs to the so-called B1 subfamily of MBLs and shares the folding of alpha beta/beta alpha sandwich, consisting of a core of beta-sheet surrounded by alpha-helices. Surprisingly, it showed a high tendency to be strongly oxidised at the catalytic cysteine located in the Cys site, Cys221, which, in the oxidised structure, becomes a cysteinesulfonic residue. Its native structure was obtained only in the presence of Tris(2-carboxyethyl)phosphine. This oxidation might be a consequence of a lower affinity for the second Zn located in the Cys site that would also explain the observed susceptibility of VIM-2 to chelating agents. This modification, if present in nature, might play a role in catalytic down-regulation. Comparison between native and oxidised VIM-2 and a predicted model of VIM-1 (which shows one residue different in the Cys site compared with VIM-2) is performed to explain the different activities and antibiotic specificities.

PubMed: 18061205
DOI: 10.1016/j.jmb.2007.11.012

Experimental method

X-RAY DIFFRACTION (1.91 Å)