Modeling the Cryo-EM Structure of the Exocyst Complex.

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. © 2023. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.

Citation

Kunrong Mei, Wei Guo. Modeling the Cryo-EM Structure of the Exocyst Complex. Methods in molecular biology (Clifton, N.J.). 2023;2557:247-262

Mesh Tags

PMID: 36512220

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