Modeling the Cryo-EM Structure of the Exocyst Complex.
Modeling the Cryo-EM Structure of the Exocyst Complex.
复制标题
模拟外囊复合体的冷冻电镜结构。
DOI：
10.1007/978-1-0716-2639-9_16
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发表时间：
2023
期刊：
影响因子：
--
通讯作者：
Guo,Wei
中科院分区：
文献类型：
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作者：
Mei,Kunrong;Guo,Wei
多亚基拴系复合体(MTCs)是一类进化上保守的大型蛋白质复合体，其功能是将细胞内的小泡从供体隔室连接到受体隔室的膜上。外囊复合体是一个八聚体MTC，它将高尔基体后分泌囊泡连接到质膜上。要了解外囊复合体的功能和调节，了解复合体的结构是至关重要的。我们已经在4.4埃分辨率下解决了包囊复合体的低温-EM结构，并用化学交联质谱仪检测了8个亚基之间的空间关系。在这里，我们描述了建模和验证胞外包囊复合体的冷冻EM结构的方法。这种方法可以为其他蛋白质复合体的建模提供指导，这些复合体的结构是在中原子到近原子分辨率下求解的。
Multi-subunit tethering complexes (MTCs) are a family of evolutionarily conserved large protein complexes that function to tether intracellular vesicles from the donor compartments to the membrane of receptor compartments. The exocyst complex is an octameric MTC that tethers the post-Golgi secretory vesicles to the plasma membrane. To learn the function and regulation of the exocyst complex, it is crucial to understand the structure of the complex. We have solved the cryo-EM structure of the exocyst complex at 4.4 Angstrom (Å) resolution and detected the spatial relationship between the eight subunits using chemical cross-linking mass spectrometry. Here, we describe the method of modeling and validating the cryo-EM structure of the exocyst complex. This method could provide a guide for modeling of other protein complexes of which the structures are solved at medium to near-atomic resolution.