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TitleCryo-EM structure of the exocyst complex.
Journal, issue, pagesNat Struct Mol Biol, Vol. 25, Issue 2, Page 139-146, Year 2018
Publish dateJan 15, 2018
AuthorsKunrong Mei / Yan Li / Shaoxiao Wang / Guangcan Shao / Jia Wang / Yuehe Ding / Guangzuo Luo / Peng Yue / Jun-Jie Liu / Xinquan Wang / Meng-Qiu Dong / Hong-Wei Wang / Wei Guo /
PubMed AbstractThe exocyst is an evolutionarily conserved octameric protein complex that mediates the tethering of post-Golgi secretory vesicles to the plasma membrane during exocytosis and is implicated in many ...The exocyst is an evolutionarily conserved octameric protein complex that mediates the tethering of post-Golgi secretory vesicles to the plasma membrane during exocytosis and is implicated in many cellular processes such as cell polarization, cytokinesis, ciliogenesis and tumor invasion. Using cryo-EM and chemical cross-linking MS (CXMS), we solved the structure of the Saccharomyces cerevisiae exocyst complex at an average resolution of 4.4 Å. Our model revealed the architecture of the exocyst and led to the identification of the helical bundles that mediate the assembly of the complex at its core. Sequence analysis suggests that these regions are evolutionarily conserved across eukaryotic systems. Additional cell biological data suggest a mechanism for exocyst assembly that leads to vesicle tethering at the plasma membrane.
External linksNat Struct Mol Biol / PubMed:29335562 / PubMed Central
MethodsEM (single particle)
Resolution4.4 Å
Structure data

6827

5yfp

EMDB-6827, PDB-5yfp:
Cryo-EM Structure of the Exocyst Complex
Method: EM (single particle) / Resolution: 4.4 Å

Source
  • Saccharomyces cerevisiae (brewer's yeast)
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
KeywordsEXOCYTOSIS / exocyst / coiled-coil

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