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Structure paper

TitleEvidence of adaptability in metal coordination geometry and active-site loop conformation among B1 metallo-beta-lactamases .
Journal, issue, pagesBiochemistry, Vol. 49, Page 7930-7938, Year 2010
Publish dateJun 25, 2009 (structure data deposition date)
AuthorsGonzalez, J.M. / Buschiazzo, A. / Vila, A.J.
External linksBiochemistry / PubMed:20677753
MethodsX-ray diffraction
Resolution1.45 - 1.74 Å
Structure data

PDB-3i0v:
Bacillus cereus metallo-beta-lactamase: apo form
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-3i11:
Cobalt-substituted metallo-beta-lactamase from Bacillus cereus
Method: X-RAY DIFFRACTION / Resolution: 1.45 Å

PDB-3i13:
Bacillus cereus Zn-dependent metallo-beta-lactamase at pH 5.8
Method: X-RAY DIFFRACTION / Resolution: 1.74 Å

PDB-3i14:
Cobalt-substituted metallo-beta-lactamase from Bacillus cereus: residue Cys168 partially oxidized
Method: X-RAY DIFFRACTION / Resolution: 1.55 Å

PDB-3i15:
Cobalt-substituted metallo-beta-lactamase from Bacillus cereus: residue Cys168 fully oxidized
Method: X-RAY DIFFRACTION / Resolution: 1.55 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-CO:
Unknown entry

ChemComp-ZN:
Unknown entry

ChemComp-GOL:
GLYCEROL

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

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