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TitleA Noncanonical Tryptophan Analogue Reveals an Active Site Hydrogen Bond Controlling Ferryl Reactivity in a Heme Peroxidase.
Journal, issue, pagesJacs Au, Vol. 1, Page 913-918, Year 2021
Publish dateFeb 13, 2020 (structure data deposition date)
AuthorsOrtmayer, M. / Hardy, F.J. / Quesne, M.G. / Fisher, K. / Levy, C. / Heyes, D.J. / Catlow, C.R.A. / de Visser, S.P. / Rigby, S.E.J. / Hay, S. / Green, A.P.
External linksJacs Au / PubMed:34337604
MethodsX-ray diffraction
Resolution1.5 - 1.7 Å
Structure data

PDB-6y1t:
The crystal structure of engineered cytochrome c peroxidase from Saccharomyces cerevisiae with a Trp51 to S-Trp51 modification
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-6y2y:
The crystal structure of engineered cytochrome c peroxidase from Saccharomyces cerevisiae with Trp51 to S-Trp51 and Trp191Phe modifications
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-1PE:
PENTAETHYLENE GLYCOL / precipitant*YM

ChemComp-HOH:
WATER

Source
  • saccharomyces cerevisiae s288c (yeast)
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
KeywordsOXIDOREDUCTASE / Peroxidase / heme / engineered / non-canonical amino acid

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