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Structure paper

TitleMetallo-beta-lactamases withstand low Zn(II) conditions by tuning metal-ligand interactions.
Journal, issue, pagesNat. Chem. Biol., Vol. 8, Page 698-700, Year 2012
Publish dateNov 12, 2009 (structure data deposition date)
AuthorsGonzalez, J.M. / Meini, M.R. / Tomatis, P.E. / Medrano Martin, F.J. / Cricco, J.A. / Vila, A.J.
External linksNat. Chem. Biol. / PubMed:22729148
MethodsX-ray diffraction
Resolution1.58 - 1.71 Å
Structure data

PDB-3knr:
Bacillus cereus metallo-beta-lactamase Cys221Asp mutant, 1 mM Zn(II)
Method: X-RAY DIFFRACTION / Resolution: 1.71 Å

PDB-3kns:
Bacillus cereus metallo-beta-lactamase Cys221Asp mutant, 20 mM Zn(II)
Method: X-RAY DIFFRACTION / Resolution: 1.58 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-ACY:
ACETIC ACID

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • bacillus cereus (bacteria)
KeywordsHYDROLASE / Metallo-beta-lactamase / Zn-dependent hydrolase / Antibiotic resistance / Metal-binding

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