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TitleFunctional Importance of Tyrosine 294 and the Catalytic Selectivity for the Bis-Fe(IV) State of MauG Revealed by Replacement of This Axial Heme Ligand with Histidine .
Journal, issue, pagesBiochemistry, Vol. 49, Page 9783-9791, Year 2010
Publish dateSep 7, 2010 (structure data deposition date)
AuthorsAbu Tarboush, N. / Jensen, L.M. / Feng, M. / Tachikawa, H. / Wilmot, C.M. / Davidson, V.L.
External linksBiochemistry / PubMed:20929212
MethodsX-ray diffraction
Resolution1.91 Å
Structure data

PDB-3orv:
Crystal Structure of the Y294H-MauG/pre-Methylamine Dehydrogenase Complex
Method: X-RAY DIFFRACTION / Resolution: 1.91 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-HEC:
HEME C

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-PGE:
TRIETHYLENE GLYCOL

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-PG4:
TETRAETHYLENE GLYCOL / precipitant*YM

ChemComp-P6G:
HEXAETHYLENE GLYCOL / precipitant*YM

ChemComp-HOH:
WATER

Source
  • paracoccus denitrificans (bacteria)
KeywordsOXIDOREDUCTASE/ELECTRON TRANSPORT / MauG / methylamine dehydrogenase / His-His heme / c-heme / quinone cofactor / OXIDOREDUCTASE-ELECTRON TRANSPORT complex

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