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TitleMechanism of action and NAD+-binding mode revealed by the crystal structure of L-histidinol dehydrogenase.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 99, Page 1859-1864, Year 2002
Publish dateOct 18, 2001 (structure data deposition date)
AuthorsBarbosa, J.A.R.G. / Sivaraman, J. / Li, Y. / Larocque, R. / Matte, A. / Schrag, J.D. / Cygler, M.
External linksProc. Natl. Acad. Sci. USA / PubMed:11842181
MethodsX-ray diffraction
Resolution1.7 - 2.1 Å
Structure data

PDB-1k75:
The L-histidinol dehydrogenase (hisD) structure implicates domain swapping and gene duplication.
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

PDB-1kae:
L-HISTIDINOL DEHYDROGENASE (HISD) STRUCTURE COMPLEXED WITH L-HISTIDINOL (SUBSTRATE), ZINC AND NAD (COFACTOR)
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-1kah:
L-HISTIDINOL DEHYDROGENASE (HISD) STRUCTURE COMPLEXED WITH L-HISTIDINE (PRODUCT), ZN AND NAD (COFACTOR)
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-1kar:
L-HISTIDINOL DEHYDROGENASE (HISD) STRUCTURE COMPLEXED WITH HISTAMINE (INHIBITOR), ZINC AND NAD (COFACTOR)
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-ZN:
Unknown entry

ChemComp-DTT:
2,3-DIHYDROXY-1,4-DITHIOBUTANE

ChemComp-HSO:
L-histidinol

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

ChemComp-IMD:
IMIDAZOLE

ChemComp-HIS:
HISTIDINE

ChemComp-HSM:
HISTAMINE / neurotransmitter, hormone*YM

Source
  • escherichia coli (E. coli)
KeywordsOXIDOREDUCTASE / L-histidinol dehydrogenase / homodimer / Rossmann fold / 4 domains / hisD / L-histidine biosynthesis / NAD cofactor / Montreal-Kingston Bacterial Structural Genomics Initiative / BSGI / Structural Genomics / ZINC

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