Structure of alcohol dehydrogenase from Entamoeba histolytica.
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.
Shimon
Linda J W
LJ
Department of Chemical Research Support, The Weizmann Institute of Science, Rehovot 76100, Israel. linda.shimon@weizmann.ac.il
Goihberg
Edi
E
Peretz
Moshe
M
Burstein
Yigal
Y
Frolow
Felix
F
D000426:Alcohol Dehydrogenase / Q000737:chemistry*; D000818:Animals; D001051:Apoenzymes / Q000737:chemistry; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D004748:Entamoeba histolytica / Q000201:enzymology*; D008958:Models, Molecular; D020836:Protein Structure, Quaternary; D015800:Protozoan Proteins / Q000737:chemistry*; D015032:Zinc / Q000737:chemistry
D001051:Apoenzymes; D015800:Protozoan Proteins; D000426:Alcohol Dehydrogenase; D015032:Zinc