Site-selective binding of Zn(II) to metallo-β-lactamase L1 from Stenotrophomonas maltophilia
- 18 February 2006
- journal article
- Published by Springer Science and Business Media LLC in JBIC Journal of Biological Inorganic Chemistry
- Vol. 11 (3), 351-358
- https://doi.org/10.1007/s00775-006-0083-z
Abstract
Extended X-ray absorption fine structure studies of the metallo-β-lactamase L1 from Stenotrophomonas maltophilia containing 1 and 2 equiv of Zn(II) and containing 2 equiv of Zn(II) plus hydrolyzed nitrocefin are presented. The data indicate that the first, catalytically dominant metal ion is bound by L1 at the consensus Zn1 site. The data further suggest that binding of the first metal helps preorganize the ligands for binding of the second metal ion. The di-Zn enzyme displays a well-defined metal–metal interaction at 3.42 Å. Reaction with the β-lactam antibiotic nitrocefin results in a product-bound species, in which the ring-opened lactam rotates in the active site to present the S1 sulfur atom of nitrocefin to one of the metal ions for coordination. The product bridges the two metal ions, with a concomitant lengthening of the Zn–Zn interaction to 3.62 Å.Keywords
This publication has 53 references indexed in Scilit:
- Antibiotic Recognition by Binuclear Metallo-β-Lactamases Revealed by X-ray CrystallographyJournal of the American Chemical Society, 2005
- Spectroscopic Studies on Cobalt(II)-Substituted Metallo-β-lactamase ImiS from Aeromonas veronii bv. sobriaBiochemistry, 2005
- Direct Evidence That the Reaction Intermediate of Metallo-β-lactamase L1 Is Metal BoundBiochemistry, 2004
- Analysis of the Importance of the Metallo-β-Lactamase Active Site Loop in Substrate Binding and CatalysisCell Chemical Biology, 2003
- Metal Ion Binding and Coordination Geometry for Wild Type and Mutants of Metallo-β-lactamase from Bacillus cereus569/H/9 (BcII)Published by Elsevier BV ,2001
- Novel Mechanism of Hydrolysis of Therapeutic β-Lactams byStenotrophomonas maltophilia L1 Metallo-β-lactamasePublished by Elsevier BV ,2001
- 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
- The crystal structure of the L1 metallo-β-lactamase from Stenotrophomonas maltophilia at 1.7 å resolutionJournal of Molecular Biology, 1998
- Spectroscopic Characterization of a Binuclear Metal Site in Bacillus cereus β-Lactamase IIBiochemistry, 1998
- Zn(II) Dependence of the Aeromonas hydrophila AE036 Metallo-β-lactamase Activity and StabilityBiochemistry, 1997