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Structure paper

TitleDetermination of the structure of Escherichia coli glyoxalase I suggests a structural basis for differential metal activation.
Journal, issue, pagesBiochemistry, Vol. 39, Page 8719-8727, Year 2000
Publish dateJul 11, 2000 (structure data deposition date)
AuthorsHe, M.M. / Clugston, S.L. / Honek, J.F. / Matthews, B.W.
External linksBiochemistry / PubMed:10913283
MethodsX-ray diffraction
Resolution1.5 - 1.9 Å
Structure data

PDB-1f9z:
CRYSTAL STRUCTURE OF THE NI(II)-BOUND GLYOXALASE I FROM ESCHERICHIA COLI
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-1fa5:
CRYSTAL STRUCTURE OF THE ZN(II)-BOUND GLYOXALASE I OF ESCHERICHIA COLI
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-1fa6:
CRYSTAL STRUCTURE OF THE CO(II)-BOUND GLYOXALASE I OF ESCHERICHIA COLI
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-1fa7:
CRYSTAL STRUCTURE OF CD(II)-BOUND GLYOXALASE I OF ESCHERICHIA COLI
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-1fa8:
CRYSTAL STRUCTURE OF THE APO FORM GLYOXALASE I OF ESCHERICHIA COLI
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-NI:
NICKEL (II) ION

ChemComp-HOH:
WATER

ChemComp-ZN:
Unknown entry

ChemComp-CO:
Unknown entry

ChemComp-CD:
Unknown entry

Source
  • escherichia coli (E. coli)
KeywordsLYASE / Beta-Alpha-Beta-Beta-Beta motif / Protein-Ni(II) complex / homodimer / Zn(II)-bound / protein-Co(II) complex / protein-Cd(II) complex / apo enzyme.

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