Hydroxyl Groups in the ββ Sandwich of Metallo-β-lactamases Favor Enzyme Activity: A Computational Protein Design Study
- 15 July 2005
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 350 (3), 395-401
- https://doi.org/10.1016/j.jmb.2005.04.044
Abstract
No abstract availableKeywords
This publication has 27 references indexed in Scilit:
- Integron Carrying a Novel Metallo-β-Lactamase Gene, bla IMP-16 , and a Fused Form of Aminoglycoside-Resistant Gene aac(6′)-30/aac(6′)-Ib′ : Report from the SENTRY Antimicrobial Surveillance ProgramAntimicrobial Agents and Chemotherapy, 2004
- Analysis of the Context Dependent Sequence Requirements of Active Site Residues in the Metallo-β-lactamase IMP-1Journal of Molecular Biology, 2004
- In vivo folding of recombinant metallo-β-lactamase L1 requires the presence of Zn(II)Protein Science, 2004
- Role of a solvent‐exposed tryptophan in the recognition and binding of antibiotic substrates for a metallo‐β‐lactamaseProtein Science, 2003
- Analysis of the Importance of the Metallo-β-Lactamase Active Site Loop in Substrate Binding and CatalysisChemistry & Biology, 2003
- Conformational splitting: A more powerful criterion for dead-end eliminationJournal of Computational Chemistry, 2000
- Amino Acid Substitutions in a Variant of IMP-1 Metallo-β-LactamaseAntimicrobial Agents and Chemotherapy, 2000
- Crystal Structure of the IMP-1 Metallo β-Lactamase from Pseudomonas aeruginosa and Its Complex with a Mercaptocarboxylate Inhibitor: Binding Determinants of a Potent, Broad-Spectrum Inhibitor,Biochemistry, 2000
- Rubredoxin Variant Folds without IronJournal of the American Chemical Society, 1999
- MOLMOL: A program for display and analysis of macromolecular structuresJournal of Molecular Graphics, 1996