Preliminary X-ray crystallographic studies of yeast Get3.
Preliminary X-ray crystallographic studies of yeast Get3.
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酵母 Get3 的 X 射线晶体学初步研究。
DOI：
10.1107/s1744309109012317
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发表时间：
2009
期刊：
影响因子：
--
通讯作者：
Sha,Bingdong
中科院分区：
文献类型：
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作者：
Hu,Junbin;Li,Jingzhi;Qian,Xinguo;Jin,Zhongmin;Fu,Zhengqing;Sha,Bingdong
尾锚定（TA）蛋白在c端含有单个跨膜结构域（TMD）。TA蛋白的翻译后插入内质网膜需要高尔基内质网转运（GET）复合体的配合，该复合体包含Get1、Get2和Get3。Get3是一种胞质atp酶，可以识别和结合TA蛋白的TMD。Get1和Get2是ER跨膜蛋白，可以招募ta结合的Get3并与之形成复合物。GET复合物执行一个能量依赖的过程，促进ta蛋白TMD插入内质网膜。为了研究GET复合物促进蛋白质插入内质网膜的机制，我们对酵母Get3进行了结晶。晶体衍射到2.7 Å分辨率使用同步加速器x射线源。晶体属于空间群P21212，晶胞参数a = 220.26, b = 112.95, c = 48.27 Å。不对称单元中有一个Get3二聚体，对应溶剂含量约为65%。
Tail-anchored (TA) proteins contain a single transmembrane domain (TMD) at the C-terminus. The post-translational insertion of TA proteins into the ER membrane requires the cooperation of the Golgi ER-trafficking (GET) complex, which contains Get1, Get2 and Get3. Get3 is a cytosolic ATPase which can recognize and bind the TMD of the TA proteins. Get1 and Get2 are ER transmembrane proteins which can recruit and form a complex with TA-bound Get3. The GET complex carries out an energy-dependent process that facilitates the insertion of the TA-protein TMD into the ER membrane. In order to investigate the mechanism by which the GET complex functions to promote protein insertion into the ER membrane, yeast Get3 has been crystallized. The crystals diffracted to 2.7 Å resolution using a synchrotron X-ray source. The crystals belonged to space group P21212, with unit-cell parameters a = 220.26, b = 112.95, c = 48.27 Å. There is one Get3 dimer in the asymmetric unit, which corresponds to a solvent content of approximately 65%.