Crystal structure of enolase from Drosophila melanogaster
Crystal structure of enolase from Drosophila melanogaster
复制标题
果蝇烯醇酶的晶体结构
DOI：
10.1107/s2053230x17004022
复制
发表时间：
2017-04-01
影响因子：
0.9
通讯作者：
Su, Zhongliang
中科院分区：
文献类型：
--
作者：
Sun, Congcong;Xu, Baokui;Su, Zhongliang
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 angstrom 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.
