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Structure paper

TitleThe Role of Invariant Amino Acid Residues at the Hydride Transfer Site of Proton-translocating Transhydrogenase.
Journal, issue, pagesJ. Biol. Chem., Vol. 281, Page 13345-13354, Year 2006
Publish dateJan 19, 2006 (structure data deposition date)
AuthorsBrondijk, T.H. / van Boxel, G.I. / Mather, O.C. / Quirk, P.G. / White, S.A. / Jackson, J.B.
External linksJ. Biol. Chem. / PubMed:16533815
MethodsX-ray diffraction
Resolution2.3 - 3.2 Å
Structure data

PDB-2fr8:
Structure of transhydrogenase (dI.R127A.NAD+)2(dIII.NADP+)1 asymmetric complex
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-2frd:
Structure of Transhydrogenase (dI.S138A.NADH)2(dIII.NADPH)1 asymmetric complex
Method: X-RAY DIFFRACTION / Resolution: 3.2 Å

PDB-2fsv:
Structure of transhydrogenase (dI.D135N.NAD+)2(dIII.E155W.NADP+)1 asymmetric complex
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-NAD:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD*YM

ChemComp-NAP:
NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

ChemComp-HOH:
WATER

ChemComp-NAI:
1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE

ChemComp-NDP:
NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

ChemComp-GOL:
GLYCEROL

Source
  • rhodospirillum rubrum (bacteria)
KeywordsOXIDOREDUCTASE / NAD(P) TRANSHYDROGENASE SUBUNITS / NAD+ / NADP+ / NADH / NADPH

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