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Structure paper

TitleDioxygen activation for the self-degradation of heme: reaction mechanism and regulation of heme oxygenase.
Journal, issue, pagesInorg. Chem., Vol. 49, Page 3602-3609, Year 2010
Publish dateJul 10, 2009 (structure data deposition date)
AuthorsMatsui, T. / Iwasaki, M. / Sugiyama, R. / Unno, M. / Ikeda-Saito, M.
External linksInorg. Chem. / PubMed:20380462
MethodsX-ray diffraction
Resolution1.5 - 2.25 Å
Structure data

PDB-3i8r:
Crystal structure of the heme oxygenase from Corynebacterium diphtheriae (HmuO) in complex with heme binding ditiothreitol (DTT)
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-3i9t:
Crystal structure of the rat heme oxygenase (HO-1) in complex with heme binding dithiothreitol (DTT)
Method: X-RAY DIFFRACTION / Resolution: 2.15 Å

PDB-3i9u:
Crystal structure of the rat heme oxygenase (HO-1) in complex with heme binding dithioerythritol (DTE)
Method: X-RAY DIFFRACTION / Resolution: 2.25 Å

Chemicals

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-SO4:
SULFATE ION

ChemComp-DTV:
(2S,3S)-1,4-DIMERCAPTOBUTANE-2,3-DIOL

ChemComp-HOH:
WATER

ChemComp-DTU:
(2R,3S)-1,4-DIMERCAPTOBUTANE-2,3-DIOL

Source
  • corynebacterium diphtheriae (bacteria)
  • rattus norvegicus (Norway rat)
KeywordsOXIDOREDUCTASE / Inhibitor / heme oxygenase / DTT / mammalian / isozyme / Endoplasmic reticulum / Heme / Iron / Metal-binding / Microsome / Phosphoprotein

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