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Structure paper

TitleMetzincin's canonical methionine is responsible for the structural integrity of the zinc-binding site
Journal, issue, pagesBiol. Chem., Vol. 390, Page 875-881, Year 2009
Publish dateMay 4, 2009 (structure data deposition date)
AuthorsOberholzer, A.E. / Bumann, M. / Hege, T. / Russo, S. / Baumann, U.
External linksBiol. Chem. / PubMed:19558324
MethodsX-ray diffraction
Resolution1.75 - 2.131 Å
Structure data

PDB-3hb2:
PrtC methionine mutants: M226I
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

PDB-3hbu:
PrtC methionine mutants: M226H DESY
Method: X-RAY DIFFRACTION / Resolution: 1.77 Å

PDB-3hbv:
PrtC methionine mutants: M226A in-house
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

PDB-3hda:
PrtC methionine mutants: M226A_DESY
Method: X-RAY DIFFRACTION / Resolution: 2.131 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-ZN:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

Source
  • erwinia chrysanthemi (bacteria)
  • synthetic construct (others)
  • unidentified (others)
KeywordsHYDROLASE / Met-turn / beta roll / zinc / Calcium / Metal-binding / Metalloprotease / Protease / Secreted / Zymogen / metzincin

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