来自酿酒酵母的Ynk1的结构。
Structure of Ynk1 from the yeast Saccharomyces cerevisiae.
作者信息
Wang Huabing, Bao Rui, Jiang Chunhui, Yang Zhu, Zhou Cong Zhao, Chen Yuxing
机构信息
Protein Research Institute, Tongji University, Shanghai 200092, People's Republic of China.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Jul 1;64(Pt 7):572-6. doi: 10.1107/S1744309108015212. Epub 2008 Jun 28.
Abstract
Nucleoside diphosphate kinase (NDPK) catalyzes the transfer of the gamma-phosphate from nucleoside triphosphates to nucleoside diphosphates. In addition to biochemical studies, a number of crystal structures of NDPK from various organisms, including both native proteins and complexes with nucleotides or nucleotide analogues, have been determined. Here, the crystal structure of Ynk1, an NDPK from the yeast Saccharomyces cerevisiae, has been solved at 3.1 A resolution. Structural analysis strongly supports the oligomerization state of this protein being hexameric rather than tetrameric.
摘要
核苷二磷酸激酶（NDPK）催化γ-磷酸基团从核苷三磷酸转移至核苷二磷酸。除生化研究外，还测定了来自多种生物体的NDPK的一些晶体结构，包括天然蛋白质以及与核苷酸或核苷酸类似物的复合物。在此，已解析出酿酒酵母NDPK Ynk1的晶体结构，分辨率为3.1埃。结构分析有力地支持了该蛋白质的寡聚化状态为六聚体而非四聚体。
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