2WGV: Crystal Structure Of The Oxa-10 V117t Mutant At Ph 6.5 Inhibited By A Chloride Ion

Citation:
Abstract
The activity of class D beta-lactamases is dependent on Lys70 carboxylation in the active site. Structural, kinetic and affinity studies show that this post-translational modification can be affected by the presence of a poor substrate such as moxalactam but also by the V117T substitution. Val117 is a strictly conserved hydrophobic residue located in the active site. In addition, inhibition of class D beta-lactamases by chloride ions is due to a competition between the side chain carboxylate of the modified Lys70 and chloride ions. Determination of the individual kinetic constants shows that the deacylation of the acyl-enzyme is the rate-limiting step for the wild-type OXA-10 beta-lactamase.
PDB ID: 2WGVDownload
MMDB ID: 82128
PDB Deposition Date: 2009/4/27
Updated in MMDB: 2010/12
Experimental Method:
x-ray diffraction
Resolution: 1.8  Å
Source Organism:
Similar Structures:
Biological Unit for 2WGV: dimeric; determined by author and by software (PISA)
Molecular Components in 2WGV
Label Count Molecule
Proteins (2 molecules)
2
Beta-lactamase Oxa-10
Molecule annotation
Chemicals (10 molecules)
1
3
2
5
3
1
4
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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