4NQ2: Structure of Zn(II)-bound metallo-beta-lactamse VIM-2 from Pseudomonas aeruginosa

Citation:
Abstract
This study examines metal binding to metallo-beta-lactamase VIM-2, demonstrating the first successful preparation of a Co(II)-substituted VIM-2 analogue. Spectroscopic studies of the half- and fully metal loaded enzymes show that both Zn(II) and Co(II) bind cooperatively, where the major species present, regardless of stoichiometry, are apo- and di-Zn (or di-Co) enzymes. We determined the di-Zn VIM-2 structure to a resolution of 1.55 A, and this structure supports results from spectroscopic studies. Kinetics, both steady-state and pre-steady-state, show that VIM-2 utilizes a mechanism that proceeds through a very short-lived anionic intermediate when chromacef is used as the substrate. Comparison with other B1 enzymes shows that those that bind Zn(II) cooperatively are better poised to protonate the intermediate on its formation, compared to those that bind Zn(II) non-cooperatively, which uniformly build up substantial amounts of the intermediate.
PDB ID: 4NQ2Download
MMDB ID: 124644
PDB Deposition Date: 2013/11/23
Updated in MMDB: 2017/12
Experimental Method:
x-ray diffraction
Resolution: 1.55  Å
Source Organism:
Similar Structures:
Biological Unit for 4NQ2: monomeric; determined by author and by software (PISA)
Molecular Components in 4NQ2
Label Count Molecule
Protein (1 molecule)
1
Beta-lactamase Class B Vim-2
Molecule annotation
Chemicals (5 molecules)
1
3
2
2
* Click molecule labels to explore molecular sequence information.

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