Insights into Class D β-Lactamases Are Revealed by the Crystal Structure of the OXA10 Enzyme from Pseudomonas aeruginosa
- 1 December 2000
- Vol. 8 (12) , 1289-1298
- https://doi.org/10.1016/s0969-2126(00)00534-7
Abstract
No abstract availableKeywords
This publication has 55 references indexed in Scilit:
- The High Resolution Crystal Structure for Class A β-Lactamase PER-1 Reveals the Bases for Its Increase in Breadth of ActivityJournal of Biological Chemistry, 2000
- The First Structural and Mechanistic Insights for Class D β-Lactamases: Evidence for a Novel Catalytic Process for Turnover of β-Lactam AntibioticsJournal of the American Chemical Society, 2000
- ESPript: analysis of multiple sequence alignments in PostScript.Bioinformatics, 1999
- X-ray Analysis of the NMC-A β-Lactamase at 1.64-Å Resolution, a Class A Carbapenemase with Broad Substrate SpecificityJournal of Biological Chemistry, 1998
- Carbapenems as inhibitors of OXA-13, a novel, integron-encoded β-lactamase in Pseudomonas aeruginosaMicrobiology, 1998
- Refinement of Macromolecular Structures by the Maximum-Likelihood MethodActa Crystallographica Section D-Biological Crystallography, 1997
- Orderly Disposition of Heterogeneous Small Subunits in D-Ribulose-1,5-bisphosphate Carboxylase/Oxygenase from SpinachPublished by Elsevier ,1996
- Crystal Structure of 6α-(Hydroxymethyl)penicillanate Complexed to the TEM-1 β-Lactamase from Escherichia coli: Evidence on the Mechanism of Action of a Novel Inhibitor Designed by a Computer-Aided ProcessJournal of the American Chemical Society, 1996
- Electrostatic analysis of TEM1 β-lactamase: effect of substrate binding, steep potential gradients and consequences of site-directed mutationsStructure, 1995
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994