Kutzenko A S, Lamzin V S, Popov V O
Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow.
FEBS Lett. 1998 Feb 13;423(1):105-9. doi: 10.1016/s0014-5793(98)00074-x.
L- and D-specific nicotinamide adenine dinucleotide (NAD)-dependent dehydrogenases map to the same structural protein superfamily as defined by the Structural Classification of Proteins (SCOP) and are based on the Rossmann fold type domains. A detailed classification of these domains is proposed using a novel diagnostic parameter of the rms per aligned pair. The catalytic domain in D-specific dehydrogenases shows a strong structural homology to the coenzyme binding domain. A topologically conserved part within the dehydrogenase superfamily reveals a supersecondary structural motif comprising the 5-stranded left-handedly twisted parallel beta-sheet with one complete and one partial Rossmann fold units and two alpha-helices, the long helix, adjacent to and running roughly parallel with the beta-sheet plane and the helix connecting two Rossmann folds.
L-和D-特异性烟酰胺腺嘌呤二核苷酸（NAD）依赖性脱氢酶与蛋白质结构分类（SCOP）所定义的相同结构蛋白超家族相关，并且基于Rossmann折叠型结构域。利用每比对对的均方根（rms）这一新型诊断参数，对这些结构域进行了详细分类。D-特异性脱氢酶中的催化结构域与辅酶结合结构域显示出很强的结构同源性。脱氢酶超家族内拓扑保守的部分揭示了一种超二级结构基序，其包含由5股左手螺旋平行β-折叠片组成，带有一个完整和一个部分Rossmann折叠单元以及两个α-螺旋，长螺旋与β-折叠片平面相邻并大致平行延伸，还有连接两个Rossmann折叠的螺旋。
