Crystallization and preliminary X-ray characterization of full-length Chlamydomonas reinhardtii centrin.
Crystallization and preliminary X-ray characterization of full-length Chlamydomonas reinhardtii centrin.
复制标题
全长莱茵衣藻中心蛋白的结晶和初步 X 射线表征。
DOI：
10.1107/s1744309108009123
复制
发表时间：
2008
期刊：
影响因子：
--
通讯作者：
Schreiter,EricR
中科院分区：
文献类型：
--
作者：
Alfaro,Elisa;Sosa,LilianaDelValle;Sanoguet,Zuleika;Pastrana-Ríos,Belinda;Schreiter,EricR
莱茵衣原体中心蛋白是EF-手型钙结合超家族的成员。它存在于基体复合体中，对鞭毛运动很重要。与EF-手家族的其他成员一样，中心蛋白以钙依赖性方式与其他蛋白相互作用并调节其功能。了解C. reinhardtii中心蛋白与其蛋白质靶相互作用，它在模型肽蜂毒肽存在下结晶，X射线衍射数据收集到2.2 μ m分辨率。 晶体为正交晶系，晶胞参数a = 52.1，B = 114.4，c = 34.8 μ m，可能属于空间群P21212。
Chlamydomonas reinhardtii centrin is a member of the EF-hand calcium-binding superfamily. It is found in the basal body complex and is important for flagellar motility. Like other members of the EF-hand family, centrin interacts with and modulates the function of other proteins in a calcium-dependent manner. To understand how C. reinhardtii centrin interacts with its protein targets, it has been crystallized in the presence of the model peptide melittin and X-ray diffraction data have been collected to 2.2 Å resolution. The crystals are orthorhombic, with unit-cell parameters a = 52.1, b = 114.4, c = 34.8 Å, and are likely to belong to space group P21212.