Structural consequences of the active site substitution Cys181 ==> Ser in metallo-beta-lactamase from Bacteroides fragilis.
Open Access
- 31 December 2008
- journal article
- Published by Wiley in Protein Science
- Vol. 8 (1) , 249-252
- https://doi.org/10.1110/ps.8.1.249
Abstract
No abstract availableKeywords
This publication has 12 references indexed in Scilit:
- Crystal structures of the cadmium‐ and mercury‐substituted metallo‐β‐lactamase from Bacteroides fragilisProtein Science, 1997
- Crystal structure of the wide-spectrum binuclear zinc β-lactamase from Bacteroides fragilisStructure, 1996
- Characterization of the Metal-Binding Sites of the β-Lactamase from Bacteroides fragilisBiochemistry, 1996
- Contribution of enzymatic properties, cell permeability, and enzyme expression to microbiological activities of beta-lactams in three Bacteroides fragilis isolates that harbor a metallo-beta-lactamase geneAntimicrobial Agents and Chemotherapy, 1994
- Biochemical characterization of the metallo-beta-lactamase CcrA from Bacteroides fragilis TAL3636Antimicrobial Agents and Chemotherapy, 1992
- Free R value: a novel statistical quantity for assessing the accuracy of crystal structuresNature, 1992
- Accurate bond and angle parameters for X-ray protein structure refinementActa Crystallographica Section A Foundations of Crystallography, 1991
- The use of an imaging proportional counter in macromolecular crystallographyJournal of Applied Crystallography, 1987
- A spectroscopic study of metal ion and ligand binding to β-lactamase IIJournal of Inorganic Biochemistry, 1980
- Zinc as a Cofactor for Cephalosporinase from Bacillus cereus 569Biochemical Journal, 1966