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Structure paper

TitleRemoving a hydrogen bond in the dimer interface of Escherichia coli manganese superoxide dismutase alters structure and reactivity.
Journal, issue, pagesBiochemistry, Vol. 40, Page 4622-4632, Year 2001
Publish dateJan 29, 2001 (structure data deposition date)
AuthorsEdwards, R.A. / Whittaker, M.M. / Whittaker, J.W. / Baker, E.N. / Jameson, G.B.
External linksBiochemistry / PubMed:11294629
MethodsX-ray diffraction
Resolution1.35 - 2.2 Å
Structure data

PDB-1i08:
CRYSTAL STRUCTURE ANALYSIS OF THE H30A MUTANT OF MANGANESE SUPEROXIDE DISMUTASE FROM E. COLI
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-1i0h:
CRYSTAL STRUCTURE OF THE E. COLI MANGANESE SUPEROXIDE DISMUTASE MUTANT Y174F AT 1.35 ANGSTROMS RESOLUTION.
Method: X-RAY DIFFRACTION / Resolution: 1.35 Å

Chemicals

ChemComp-MN:
Unknown entry

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsOXIDOREDUCTASE / manganese superoxide dismutase / mutant / h30a / hydrogen bond / reactivity / Y174F mutant

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