Sun Congcong, Xu Baokui, Liu Xueyan, Zhang Zhen, Su Zhongliang
College of Chemical Engineering, Qingdao University of Science and Technology, Qingdao, Shandong 266042, People's Republic of China.
Jianghuai College, Anhui University, Hefei, Anhui 230039, People's Republic of China.
Acta Crystallogr F Struct Biol Commun. 2017 Apr 1;73(Pt 4):228-234. doi: 10.1107/S2053230X17004022. Epub 2017 Mar 22.
Enolase is an important enzyme in glycolysis and various biological processes. Its dysfunction is closely associated with diseases. Here, the enolase from Drosophila melanogaster (DmENO) was purified and crystallized. A crystal of DmENO diffracted to 2.0 Å resolution and belonged to space group R32. The structure was solved by molecular replacement. Like most enolases, DmENO forms a homodimer with conserved residues in the dimer interface. DmENO possesses an open conformation in this structure and contains conserved elements for catalytic activity. This work provides a structural basis for further functional and evolutionary studies of enolase.
烯醇化酶是糖酵解和各种生物过程中的一种重要酶。其功能障碍与疾病密切相关。在此，对黑腹果蝇的烯醇化酶（DmENO）进行了纯化和结晶。DmENO的晶体衍射分辨率达到2.0 Å，属于R32空间群。通过分子置换法解析了其结构。与大多数烯醇化酶一样，DmENO在二聚体界面形成具有保守残基的同型二聚体。在此结构中，DmENO具有开放构象，并包含催化活性的保守元件。这项工作为烯醇化酶的进一步功能和进化研究提供了结构基础。
