5YFP

Cryo-EM Structure of the Exocyst Complex

Summary for 5YFP

• Entry DOI: 10.2210/pdb5yfp/pdb
• EMDB information: 6827
• Descriptor: Exocyst complex component SEC3, Exocyst complex component SEC5, Exocyst complex component SEC6, ... (8 entities in total)
• Functional Keywords: exocyst, coiled-coil, exocytosis
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); More
• Total number of polymer chains: 8
• Total formula weight: 845691.45

Authors

Mei, K.,Li, Y.,Wang, S.,Shao, G.,Wang, J.,Ding, Y.,Luo, G.,Yue, P.,Liu, J.J.,Wang, X.,Dong, M.Q.,Guo, W.,Wang, H.W. (deposition date: 2017-09-21, release date: 2018-01-31, Last modification date: 2024-03-27)

Primary citation

Mei, K.,Li, Y.,Wang, S.,Shao, G.,Wang, J.,Ding, Y.,Luo, G.,Yue, P.,Liu, J.J.,Wang, X.,Dong, M.Q.,Wang, H.W.,Guo, W.
Cryo-EM structure of the exocyst complex
Nat. Struct. Mol. Biol., 25:139-146, 2018

PubMed Abstract: 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.

PubMed: 29335562
DOI: 10.1038/s41594-017-0016-2

Experimental method

ELECTRON MICROSCOPY (4.4 Å)