4uam

1.8 Angstrom crystal structure of IMP-1 metallo-beta-lactamase with a mixed iron-zinc center in the active site

spinqualitylabelsall models 4uam, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4uam is a 4 chain structure with sequence from Pseudomonas aeruginosa NCGM2.S1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: CSD, FE, FLC, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Heterodinuclear metalloenzymes are an important class of metalloproteins, but determining the location of the different metal ions can be difficult. Herein we present a new NMR spectroscopy method that uses pseudocontact shifts (PCS) to achieve this without assumptions about the coordinating ligands. The approach is illustrated with the dinuclear [FeZn] complex of IMP-1, which is a prototypical metallo-beta-lactamase (MbetaL) that confers resistance to beta-lactam antibiotics. Results from single-crystal X-ray diffraction were compromised by degradation during crystallization. With [GaZn]-IMP-1 as diamagnetic reference, the PCSs unambiguously identified the iron binding site in fresh samples of [FeZn]-IMP-1, even though the two metal centers are less than 3.8 A apart and the iron is high-spin Fe3+ , which produces only small PCSs. [FeZn]-MbetaLs may be important drug targets, as [FeZn]-IMP-1 is enzymatically active and readily produced in the presence of small amounts of Fe3+ . Iron(III) Located in the Dinuclear Metallo-beta-Lactamase IMP-1 by Pseudocontact Shifts.,Carruthers TJ, Carr PD, Loh CT, Jackson CJ, Otting G Angew Chem Int Ed Engl. 2014 Oct 15. doi: 10.1002/anie.201408693. PMID:25320022 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta-lactamase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA