5ctn

Structure of BPu1 beta-lactamaseStructure of BPu1 beta-lactamase

Structural highlights 5ctn is a 2 chain structure with sequence from Bacillus pumilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.35Å Ligands: , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A8FFI9_BACP2 Publication Abstract from PubMed Production of beta-lactamases of one of four molecular classes (A, B, C and D) is the major mechanism of bacterial resistance to beta-lactams, the largest class of antibiotics, which have saved countless lives since their inception 70 years ago. Although several hundred efficient class D enzymes have been identified in Gram-negative pathogens over the last four decades, none have been reported in Gram-positive bacteria. Here we demonstrate that efficient class D beta-lactamases capable of hydrolyzing a wide array of beta-lactam substrates are widely disseminated in various species of environmental Gram-positive organisms. Class D enzymes of Gram-positive bacteria have a distinct structural architecture and employ a unique substrate-binding mode that is quite different from that of all currently known class A, C and D beta-lactamases. These enzymes thus constitute a previously unknown reservoir of novel antibiotic-resistance enzymes. Class D beta-lactamases do exist in Gram-positive bacteria.,Toth M, Antunes NT, Stewart NK, Frase H, Bhattacharya M, Smith CA, Vakulenko SB Nat Chem Biol. 2015 Nov 9. doi: 10.1038/nchembio.1950. PMID:26551395 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta-lactamase 3D structures

spinqualitylabelsall models 5ctn, resolution 1.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image