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Crystallisation and crystallographic investigations of cod alcohol dehydrogenase class I and class III enzymes
Author(s) -
Ramaswamy S.,
El-Ahmad Mustafa,
Danielsson Olle,
Jörnvall Hans,
Eklund Hans
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00746-2
Subject(s) - dimer , monoclinic crystal system , alcohol dehydrogenase , chemistry , stereochemistry , crystallography , molecular replacement , enzyme , molecule , crystallization , oxidoreductase , crystal structure , biochemistry , organic chemistry
Cod liver alcohol dehydrogenase of class‐hybrid properties has been crystallized as an NAD + —pyrazole complex in the monoclinic space group P2 1 with cell dimensions a = 103.3 Å, b = 47.4 Å, c = 80.7 Å, β = 104.6°, and with one dimer in the asymmetric unit. The position of the dimer molecule in the crystal was determined by molecular replacement methods at 3.0 Å resolution. The successful search model was the poly‐alanine structure of the horse enzyme. Side chains were then replaced according to the amino acid sequence of the cod enzyme, and the structure has been refined at 2.8 Å to an R ‐factor of 0.26. Cod liver class III alcohol dehydrogenase crystallizes in the monoclinic space group C2 with cell dimensions a = 127.5 Å, b = 76.6 Å, c = 93.4 Å, β = 99.4° and with probably one dimer in the asymmetric unit.