3KNS

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

Summary for 3KNS

Entry DOI	10.2210/pdb3kns/pdb
Related	1bc2 1bvt 3knr
Descriptor	Beta-lactamase 2, ZINC ION, SULFATE ION, ... (6 entities in total)
Functional Keywords	metallo-beta-lactamase, zn-dependent hydrolase, antibiotic resistance, hydrolase, metal-binding
Biological source	Bacillus cereus
Cellular location	Periplasm : P04190
Total number of polymer chains	4
Total formula weight	101762.19
Authors	Medrano Martin, F.J.,Gonzalez, J.M.,Vila, A.J. (deposition date: 2009-11-12, release date: 2010-11-24, Last modification date: 2024-02-21)
Primary citation	Gonzalez, J.M.,Meini, M.R.,Tomatis, P.E.,Medrano Martin, F.J.,Cricco, J.A.,Vila, A.J. Metallo-beta-lactamases withstand low Zn(II) conditions by tuning metal-ligand interactions. Nat.Chem.Biol., 8:698-700, 2012 Cited by PubMed Abstract: A number of multiresistant bacterial pathogens inactivate antibiotics by producing Zn(II)-dependent β-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. PubMed: 22729148 DOI: 10.1038/nchembio.1005 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.58 Å)

Structure validation