Crystal structure of the IMP-1 metallo beta-lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate inhibitor: binding determinants of a potent, broad-spectrum inhibitor.
- N. Concha, C. Janson, S. Abdel-Meguid
- Chemistry, BiologyBiochemistry
- 25 March 2000
A unique mode of binding of the mercaptocarboxylate inhibitor in the enzyme active site provides a binding model for metallo beta-lactamase inhibition with utility for future drug design.
The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold.
- A. Carfi, S. Pares, O. Dideberg
- Chemistry, BiologyEMBO Journal
- 1995
The 3-D structure of Bacillus cereus (569/H/9) beta-lactamase (EC 3.5.6) has been solved and an approximate internal molecular symmetry is found, with a 2-fold axis passing roughly through the zinc ion and suggesting a possible gene duplication.
A metallo-beta-lactamase enzyme in action: crystal structures of the monozinc carbapenemase CphA and its complex with biapenem.
- G. Garau, C. Bebrone, C. Anne, M. Galleni, J. Frère, O. Dideberg
- Biology, ChemistryJournal of Molecular Biology
- 28 January 2005
Chromosome-Encoded CTX-M-3 from Kluyvera ascorbata: a Possible Origin of Plasmid-Borne CTX-M-1-Derived Cefotaximases
- M. M. Rodríguez, P. Power, G. Gutkind
- BiologyAntimicrobial Agents and Chemotherapy
- 1 December 2004
ABSTRACT A gene identical to plasmid-borne blaCTX-M-3 is present in the chromosome of one Kluyvera ascorbata strain. It is associated with a structure including an inverted repeat right and an open…
Biochemical and Structural Characterization of the Subclass B1 Metallo-β-Lactamase VIM-4
- P. Lassaux, D. Traore, M. Galleni
- BiologyAntimicrobial Agents and Chemotherapy
- 13 December 2010
Study of the thermal stability and the activity of the holo- and apo-VIM-4 enzymes revealed that Zn2+ ions have a pronounced stabilizing effect on the enzyme and are necessary for preserving the structure.
Standard Numbering Scheme for Class B β-Lactamases
- M. Galleni, J. Lamotte‐Brasseur, G. Rossolini, J. Spencer, O. Dideberg, J. Frère
- BiologyAntimicrobial Agents and Chemotherapy
- 1 March 2001
This work proposes a scheme developed through a collaborative approach that preserves traditional numbering of catalytically important residues, is adaptable to new variants or enzymes yet to be discovered and includes a variation for genetic and epidemiological applications.
β-Lactamase Inhibitors Derived from Single-Domain Antibody Fragments Elicited in the Camelidae
- K. Conrath, M. Lauwereys, S. Muyldermans
- Biology, ChemistryAntimicrobial Agents and Chemotherapy
- 1 October 2001
Addition of the VHHs to the TEM-1 β-lactamase, expressed on the surface of bacteria, leads to a higher ampicillin sensitivity of the bacteria, which could generate multiple potent inhibitors for all types of β- lactamases.
Biochemical Characterization of the Pseudomonas aeruginosa 101/1477 Metallo-β-Lactamase IMP-1 Produced byEscherichia coli
- N. Laraki, N. Franceschini, M. Galleni
- BiologyAntimicrobial Agents and Chemotherapy
- 1 April 1999
The blaIMP gene coding for the IMP-1 metallo-β-lactamase produced by a Pseudomonas aeruginosaclinical isolate was overexpressed via a T7 expression system in Escherichia coli BL21(DE3), and its product was purified to homogeneity with a final yield of 35 mg/liter of culture.
Metallo-beta-lactamases as emerging resistance determinants in Gram-negative pathogens: open issues.
- G. Cornaglia, M. Akova, G. Rossolini
- MedicineInternational Journal of Antimicrobial Agents
- 1 April 2007
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