2WHG: Crystal Structure Of The Di-Zinc Metallo-Beta-Lactamase Vim- 4 From Pseudomonas Aeruginosa

The metallo-beta-lactamase VIM-4, mainly found in Pseudomonas aeruginosa or Acinetobacter baumannii, was produced in Escherichia coli and characterized by biochemical and X-ray techniques. A detailed kinetic study performed in the presence of Zn(2)+ at concentrations ranging from 0.4 to 100 muM showed that VIM-4 exhibits a kinetic profile similar to the profiles of VIM-2 and VIM-1. However, VIM-4 is more active than VIM-1 against benzylpenicillin, cephalothin, nitrocefin, and imipenem and is less active than VIM-2 against ampicillin and meropenem. The crystal structure of the dizinc form of VIM-4 was solved at 1.9 A. The sole difference between VIM-4 and VIM-1 is found at residue 228, which is Ser in VIM-1 and Arg in VIM-4. This substitution has a major impact on the VIM-4 catalytic efficiency compared to that of VIM-1. In contrast, the differences between VIM-2 and VIM-4 seem to be due to a different position of the flapping loop and two substitutions in loop 2. Study of the thermal stability and the activity of the holo- and apo-VIM-4 enzymes revealed that Zn(2)+ ions have a pronounced stabilizing effect on the enzyme and are necessary for preserving the structure.
PDB ID: 2WHGDownload
MMDB ID: 82129
PDB Deposition Date: 2009/5/5
Updated in MMDB: 2010/12
Experimental Method:
x-ray diffraction
Resolution: 1.9  Å
Source Organism:
Similar Structures:
Biological Unit for 2WHG: monomeric; determined by author and by software (PISA)
Molecular Components in 2WHG
Label Count Molecule
Protein (1 molecule)
Vim-4 Metallo-beta-lactamase
Molecule annotation
Chemicals (3 molecules)
* Click molecule labels to explore molecular sequence information.

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