1y9a

Alcohol Dehydrogenase from Entamoeba histolotica in complex with cacodylateAlcohol Dehydrogenase from Entamoeba histolotica in complex with cacodylate

Publication Abstract from PubMed

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The structure of the apo form of alcohol dehydrogenase from a single-cell eukaryotic source, Entamoeba histolytica, has been determined at 1.8 A. To date, bacterial and archeal alcohol dehydrogenases, which are biologically active as tetramers, have crystallized with tetramers in the asymmetric unit. However, the current structure has one independent dimer per asymmetric unit and the full tetramer is generated by application of the crystallographic twofold symmetry element. This structure reveals that many of the crystallization and cryoprotection components, such as cacodylate, ethylene glycol, zinc ions and acetate, have been incorporated. These crystallization solution elements are found within the molecule and at the packing interfaces as an integral part of the three-dimensional arrangements of the tetramers. In addition, an unexpected modification of aspartic acid to O-carboxysulfanyl-4-oxo-L-homoserine was found at residue 245.

Structure of alcohol dehydrogenase from Entamoeba histolytica., Shimon LJ, Goihberg E, Peretz M, Burstein Y, Frolow F, Acta Crystallogr D Biol Crystallogr. 2006 May;62(Pt 5):541-7. Epub 2006, Apr 19. PMID:16627948

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this StructureAbout this Structure

1y9a is a 2 chain structure of Alcohol dehydrogenase with sequence from Entamoeba histolytica. Full crystallographic information is available from OCA.

See AlsoSee Also

• Alcohol dehydrogenase
• Alcohol dehydrogenase from Entamoeba histolytica
• Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-294 of T. brockii ADH by E. histolytica ADH
• Chimeras of alcohol dehydrogenases
• D275P mutant of alcohol dehydrogenase from protozoa Entamoeba histolytica
• Tetrameric alcohol dehydrogenases