5ls3 | pdb_00005ls3

Crystal structure of metallo-beta-lactamase SPM-1 with Y58C mutation

spinqualitylabelsall models 5ls3, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ls3 is a 2 chain structure with sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.754Å Ligands: ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8G9Q0_PSEAI Publication Abstract from PubMed Resistance to beta-lactam antibiotics mediated by metallo-beta-lactamases (MBLs) is a growing problem. We describe the use of protein-observe 19 F-NMR (PrOF NMR) to study the dynamics of the Sao Paulo MBL (SPM-1) from beta-lactam-resistant Pseudomonas aeruginosa. Cysteinyl variants on the alpha3 and L3 regions, which flank the di-ZnII active site, were selectively 19 F-labeled using 3-bromo-1,1,1-trifluoroacetone. The PrOF NMR results reveal roles for the mobile alpha3 and L3 regions in the binding of both inhibitors and hydrolyzed beta-lactam products to SPM-1. These results have implications for the mechanisms and inhibition of MBLs by beta-lactams and non-beta-lactams and illustrate the utility of PrOF NMR for efficiently analyzing metal chelation, identifying new binding modes, and studying protein binding from a mixture of equilibrating isomers. 19 F-NMR Reveals the Role of Mobile Loops in Product and Inhibitor Binding by the Sao Paulo Metallo-beta-Lactamase.,Abboud MI, Hinchliffe P, Brem J, Macsics R, Pfeffer I, Makena A, Umland KD, Rydzik AM, Li GB, Spencer J, Claridge TD, Schofield CJ Angew Chem Int Ed Engl. 2017 Mar 2. doi: 10.1002/anie.201612185. PMID:28252254 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