Ramaswamy S, el-Ahmad M, Danielsson O, Jörnvall H, Eklund H
Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala.
FEBS Lett. 1994 Aug 15;350(1):122-4. doi: 10.1016/0014-5793(94)00746-2.
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 A, b = 47.4 A, c = 80.7 A, beta = 104.6 degrees, 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 A 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 A 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 A, b = 76.6 A, c = 93.4 A, beta = 99.4 degrees and with probably one dimer in the asymmetric unit.
具有类杂交特性的鳕鱼肝乙醇脱氢酶已结晶为NAD(+)-吡唑复合物，属于单斜晶系空间群P2(1)，晶胞参数a = 103.3 Å，b = 47.4 Å，c = 80.7 Å，β = 104.6°，不对称单元中有一个二聚体。通过分子置换法在3.0 Å分辨率下确定了二聚体分子在晶体中的位置。成功的搜索模型是马酶的聚丙氨酸结构。然后根据鳕酶的氨基酸序列替换侧链，并将结构在2.8 Å分辨率下精修至R因子为0.26。鳕鱼肝Ⅲ类乙醇脱氢酶结晶于单斜晶系空间群C2，晶胞参数a = 127.5 Å，b = 76.6 Å，c = 93.4 Å，β = 99.4°，不对称单元中可能有一个二聚体。
