2WGW

Crystal structure of the OXA-10 V117T mutant at pH 8.0

Summary for 2WGW

• Entry DOI: 10.2210/pdb2wgw/pdb
• Related: 1E3U 1E4D 1EWZ 1FOF 1K4E 1K4F 1K54 1K55 1K56 1K57 1K6R 1K6S 2WGI 2WGV 2WKH 2WKI
• Descriptor: BETA-LACTAMASE OXA-10, SULFATE ION, GLYCEROL, ... (5 entities in total)
• Functional Keywords: antibiotic resistance, transposable, hydrolase
• Biological source: PSEUDOMONAS AERUGINOSA; More
• Total number of polymer chains: 2
• Total formula weight: 56685.12

Authors

Vercheval, L.,Kerff, F.,Bauvois, C.,Sauvage, E.,Guiet, R.,Charlier, P.,Galleni, M. (deposition date: 2009-04-27, release date: 2010-05-19, Last modification date: 2023-12-13)

Primary citation

Vercheval, L.,Bauvois, C.,Di Paolo, A.,Borel, F.,Ferrer, J.L.,Sauvage, E.,Matagne, A.,Frere, J.M.,Charlier, P.,Galleni, M.,Kerff, F.
Three Factors that Modulate the Activity of Class D Beta-Lactamases and Interfere with the Post-Translational Carboxylation of Lys70.
Biochem.J., 432:495-, 2010

PubMed Abstract: The activity of class D β-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 β-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 β-lactamase.

PubMed: 21108605
DOI: 10.1042/BJ20101122

Experimental method

X-RAY DIFFRACTION (1.8 Å)