Buehner M, Ford G C, Moras D, Olsen K W, Rossman M G
Proc Natl Acad Sci U S A. 1973 Nov;70(11):3052-4. doi: 10.1073/pnas.70.11.3052.
A 3.0-A resolution electron density map of lobster glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12) was computed. The essentially single isomorphous replacement map was very substantially improved by averaging subunits. NAD binds in an open conformation at sites close to subunit interfaces. The coenzyme binding portion of the enzyme has almost the same fold as the corresponding portion of lactate dehydrogenase (EC 1.1.1.27). The presence of this structure in the five enzymes, analyzed so far, that use nucleotide coenzymes might indicate a fundamental primordial structural element.
计算出了龙虾甘油醛-3-磷酸脱氢酶（EC 1.2.1.12）的3.0埃分辨率电子密度图。通过对亚基进行平均，基本的单对同晶置换图得到了显著改善。NAD以开放构象结合在靠近亚基界面的位点。该酶的辅酶结合部分与乳酸脱氢酶（EC 1.1.1.27）的相应部分具有几乎相同的折叠结构。在目前已分析的五种使用核苷酸辅酶的酶中都存在这种结构，这可能表明存在一个基本的原始结构元件。
