1Y9A

Alcohol Dehydrogenase from Entamoeba histolotica in complex with cacodylate

Summary for 1Y9A

• Entry DOI: 10.2210/pdb1y9a/pdb
• Descriptor: NADP-dependent alcohol dehydrogenase, ZINC ION, CACODYLATE ION, ... (7 entities in total)
• Functional Keywords: metal-binding, nadp, oxidoreductase
• Biological source: Entamoeba histolytica
• Cellular location: Cytoplasm: P35630
• Total number of polymer chains: 2
• Total formula weight: 78407.94

Authors

Shimon, L.J.,Peretz, M.,Goihberg, E.,Burstein, Y.,Frolow, F. (deposition date: 2004-12-15, release date: 2006-01-17, Last modification date: 2025-03-26)

Primary citation

Shimon, L.J.,Goihberg, E.,Peretz, M.,Burstein, Y.,Frolow, F.
Structure of alcohol dehydrogenase from Entamoeba histolytica.
Acta Crystallogr.,Sect.D, 62:541-547, 2006

PubMed Abstract: 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.

PubMed: 16627948
DOI: 10.1107/S0907444906009292

Experimental method

X-RAY DIFFRACTION (1.81 Å)