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Structure paper

TitleSteps in reductive activation of the disulfide-generating enzyme Ero1p
Journal, issue, pagesProtein Sci., Vol. 19, Page 1863-1876, Year 2010
Publish dateMar 8, 2010 (structure data deposition date)
AuthorsHeldman, N. / Vonshak, O. / Sevier, C.S. / Vitu, E. / Mehlman, T. / Fass, D.
External linksProtein Sci. / PubMed:20669236
MethodsX-ray diffraction
Resolution1.85 - 3.2 Å
Structure data

PDB-3m31:
Structure of the C150A/C295A mutant of S. cerevisiae Ero1p
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-3nvj:
Crystal structure of the C143A/C166A mutant of Ero1p
Method: X-RAY DIFFRACTION / Resolution: 3.2 Å

Chemicals

ChemComp-NEN:
1-ETHYL-PYRROLIDINE-2,5-DIONE

ChemComp-FAD:
FLAVIN-ADENINE DINUCLEOTIDE / FAD*YM

ChemComp-CD:
Unknown entry

ChemComp-HOH:
WATER

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsOXIDOREDUCTASE / disulfide mutant / Disulfide bond / Electron transport / Endoplasmic reticulum / FAD / Flavoprotein / Glycoprotein / Membrane / Redox-active center / Transport / flavoenzyme / disulfide bonds / ER

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