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Structure paper

TitleCrystal Structures of CO and NO Adducts of MauG in Complex with Pre-Methylamine Dehydrogenase: Implications for the Mechanism of Dioxygen Activation.
Journal, issue, pagesBiochemistry, Vol. 50, Page 2931-2938, Year 2011
Publish dateDec 10, 2010 (structure data deposition date)
AuthorsYukl, E.T. / Goblirsch, B.R. / Davidson, V.L. / Wilmot, C.M.
External linksBiochemistry / PubMed:21355604
MethodsX-ray diffraction
Resolution2.11 - 2.22 Å
Structure data

PDB-3pxs:
Crystal Structure of Diferrous MauG in Complex with Pre-Methylamine Dehydrogenase:
Method: X-RAY DIFFRACTION / Resolution: 2.22 Å

PDB-3pxt:
Crystal Structure of Ferrous CO Adduct of MauG in Complex with Pre-Methylamine Dehydrogenase
Method: X-RAY DIFFRACTION / Resolution: 2.16 Å

PDB-3pxw:
Crystal Structure of Ferrous NO Adduct of MauG in Complex with Pre-Methylamine Dehydrogenase
Method: X-RAY DIFFRACTION / Resolution: 2.11 Å

Chemicals

ChemComp-NA:
Unknown entry

ChemComp-HEC:
HEME C

ChemComp-CA:
Unknown entry

ChemComp-ACT:
ACETATE ION

ChemComp-PG4:
TETRAETHYLENE GLYCOL / precipitant*YM

ChemComp-PG6:
1-(2-METHOXY-ETHOXY)-2-{2-[2-(2-METHOXY-ETHOXY]-ETHOXY}-ETHANE

ChemComp-HOH:
WATER

ChemComp-CMO:
CARBON MONOXIDE

ChemComp-NO:
NITRIC OXIDE

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-PGE:
TRIETHYLENE GLYCOL

Source
  • paracoccus denitrificans (bacteria)
KeywordsOXIDOREDUCTASE/ELECTRON TRANSPORT / Oxidoreductase / electron transport / periplasmic space / OXIDOREDUCTASE-ELECTRON TRANSPORT complex / electron transfer

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