2WKI: Crystal Structure Of The Oxa-10 K70c Mutant At Ph 7.0

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: 2WKIDownload
MMDB ID: 84287
PDB Deposition Date: 2009/6/11
Updated in MMDB: 2010/12
Experimental Method:
x-ray diffraction
Resolution: 2.1  Å
Source Organism:
Similar Structures:
Biological Unit for 2WKI: dimeric; determined by author and by software (PISA)
Molecular Components in 2WKI
Label Count Molecule
Proteins (2 molecules)
Beta-lactamase Oxa-10
Molecule annotation
Chemicals (18 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB