1.1.1.23: histidinol dehydrogenase

This is an abbreviated version, for detailed information about histidinol dehydrogenase, go to the full flat file.

Reaction

L-Histidinol
+ 2 NAD+ +
H2O
=
L-histidine
+ 2 NADH + 3 H+

Synonyms

BN980_GECA03s06082g, BsHDH, GcHDH, HDH, HIS4 protein, HisD, histidinol dehydrogenase, HLDase, L-histidinol dehydrogenase

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.23 histidinol dehydrogenase

Crystallization

Crystallization on EC 1.1.1.23 - histidinol dehydrogenase

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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant detagged enzyme mutant C366S, in apoform or bound to inhibitor (3S)-3-amino-1-[4-(benzyloxy)phenyl]-4-(1H-imidazol-4-yl)butan-2-one, hanging drop vapor diffusion method, protein solution containing 50 mM Tris-HCl, 150 mM NaCl, and 1 mM DTT, as well as 1 mM ZnCl2 and 20 mM inhibitor 1, is mixed with reservoir solution containing 25% PEG 3350, 0.1 M HEPES pH 8, 0.25 M NaCl, 20C, equilibration against 1 ml of reservoir solution, method optimzation, X-ray diffraction structure determination and analysis at 1.90 A resolution, molecular replacement and modelling
15.4 mg/ml purified recombinant detagged enzyme alone or complexed with L-histidinol, L-histamine, or L-histidine or Zn2+ and NAD+, in 20 mM Tris-HCl, pH 7.5, 0.2 M NaCl, 5 mM DTT, 1 mM ligand, hanging drop vapour diffusion method, 18C, 0.002 ml protein solution with 0.004 ml reservoir solution, containing 20% w/v PEG 3350, 7% v/v glycerol, 0.1 M imidazole-malic acid, pH 5.5, 0.2 M ammonium sulfate, 2 weeks, macroseeding for larger crystals, transfer to sodium acetate, pH 5.5, to eliminate the inhibiting imidazole, X-ray diffraction structure determination and analysis at 2.2 A resolution, modelling
-
crystal structure determination of HDH in its native state and with several substrates and Zn2+. the NAD+ molecule is crystallized with L-histidinol into the active site. In the apo structure, the Zn2+ coordination is tetrahedral, while it is octahedral in the inhibitor/enzyme complex
-
only a C366S mutant allows crystallization to proceed, probably forbidding oxidation/reduction of the native enzyme at this position, molecular replacement using the structure of the Escherichia coli enzyme. In the apo structure, the Zn2+ coordination is tetrahedral, while it is octahedral in the inhibitor/enzyme complex
-
1.6-2.0 mM ammonium sulfate solution at 4C, pH 6.5, space group C2, monoclinic
-