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Structure paper

TitleThermal stabilization of the protozoan Entamoeba histolytica alcohol dehydrogenase by a single proline substitution
Journal, issue, pagesProteins, Vol. 72, Page 711-719, Year 2008
Publish dateNov 12, 2006 (structure data deposition date)
AuthorsGoihberg, E. / Dym, O. / Tel-Or, S. / Shimon, L. / Frolow, F. / Peretz, M. / Burstein, Y.
External linksProteins / PubMed:18260103
MethodsX-ray diffraction
Resolution1.77 - 2.8 Å
Structure data

PDB-2nvb:
Contribution of Pro275 to the Thermostability of the Alcohol Dehydrogenases (ADHs)
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-2oui:
D275P mutant of alcohol dehydrogenase from protozoa Entamoeba histolytica
Method: X-RAY DIFFRACTION / Resolution: 1.77 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-NAP:
NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

ChemComp-NO3:
NITRATE ION

ChemComp-CAC:
CACODYLATE ION

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-PGE:
TRIETHYLENE GLYCOL

ChemComp-1PE:
PENTAETHYLENE GLYCOL / precipitant*YM

ChemComp-CL:
Unknown entry

ChemComp-PG4:
TETRAETHYLENE GLYCOL / precipitant*YM

ChemComp-HOH:
WATER

Source
  • thermoanaerobacter brockii (bacteria)
  • entamoeba histolytica (eukaryote)
KeywordsOXIDOREDUCTASE / Rossmann fold / Structural Genomics / Israel Structural Proteomics Center / ISPC / Tetramer / METAL-BINDING / NADP / P275D MUTATION / cacodylate ion / thermosatbility

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