Structure of alcohol dehydrogenase from Entamoeba histolytica

Acta Crystallographica. Section D, Biological Crystallography
Linda J W ShimonFelix Frolow

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.

Citations

Feb 24, 2010·Applied Microbiology and Biotechnology·Manish Kumar TiwariJung-Kul Lee
Sep 14, 2010·Cellular and Molecular Life Sciences : CMLS·Sergio PortéXavier Parés
May 27, 2015·Biomedical Papers of the Medical Faculty of the University Palacký, Olomouc, Czechoslovakia·Miroslav Pohanka

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