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Structure paper

TitleMutagenesis of tryptophan199 suggests that hopping is required for MauG-dependent tryptophan tryptophylquinone biosynthesis.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 108, Page 16956-16961, Year 2011
Publish dateApr 19, 2011 (structure data deposition date)
AuthorsTarboush, N.A. / Jensen, L.M. / Yukl, E.T. / Geng, J. / Liu, A. / Wilmot, C.M. / Davidson, V.L.
External linksProc. Natl. Acad. Sci. USA / PubMed:21969534
MethodsX-ray diffraction
Resolution1.72 - 2.13 Å
Structure data

PDB-3rlm:
Structure of the W199F MauG/pre-Methylamine Dehydrogenase complex after treatment with hydrogen peroxide
Method: X-RAY DIFFRACTION / Resolution: 2.13 Å

PDB-3rmz:
Crystal Structure of the W199F-MauG/pre-Methylamine Dehydrogenase Complex
Method: X-RAY DIFFRACTION / Resolution: 1.72 Å

PDB-3rn0:
Crystal Structure of the W199K-MauG/pre-Methylamine Dehydrogenase Complex
Method: X-RAY DIFFRACTION / Resolution: 1.91 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-HEC:
HEME C

ChemComp-PGE:
TRIETHYLENE GLYCOL

ChemComp-ACT:
ACETATE ION

ChemComp-HOH:
WATER

ChemComp-NA:
Unknown entry

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-PG4:
TETRAETHYLENE GLYCOL / precipitant*YM

ChemComp-P6G:
HEXAETHYLENE GLYCOL / precipitant*YM

ChemComp-MES:
2-(N-MORPHOLINO)-ETHANESULFONIC ACID / pH buffer*YM

Source
  • paracoccus denitrificans (bacteria)
KeywordsELECTRON TRANSPORT / oxidoreductase / Oxidoreductase/electron transport / MauG / methylamine dehydrogenase / c-heme / quinone cofactor / Oxidoreductase-electron transport complex

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