3kns

Bacillus cereus metallo-beta-lactamase Cys221Asp mutant, 20 mM Zn(II)Bacillus cereus metallo-beta-lactamase Cys221Asp mutant, 20 mM Zn(II)

Structural highlights 3kns is a 4 chain structure with sequence from Atcc 14579. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: , , , Related: 1bvt, 1bc2, 3knr Gene: blm (ATCC 14579) Activity: Beta-lactamase, with EC number 3.5.2.6 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [BLA2_BACCE] Can hydrolyze carbapenem compounds. Publication Abstract from PubMed A number of multiresistant bacterial pathogens inactivate antibiotics by producing Zn(II)-dependent beta-lactamases. We show that metal uptake leading to an active dinuclear enzyme in the periplasmic space of Gram-negative bacteria is ensured by a cysteine residue, an unusual metal ligand in oxidizing environments. Kinetic, structural and affinity data show that such Zn(II)-cysteine interaction is an adaptive trait that tunes the metal binding affinity, thus enabling antibiotic resistance at restrictive Zn(II) concentrations. Metallo-beta-lactamases withstand low Zn(II) conditions by tuning metal-ligand interactions.,Gonzalez JM, Meini MR, Tomatis PE, Martin FJ, Cricco JA, Vila AJ Nat Chem Biol. 2012 Jun 24. doi: 10.1038/nchembio.1005. PMID:22729148 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta-lactamase

spinqualitylabelsall models 3kns, resolution 1.58Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image