5YFP

Cryo-EM Structure of the Exocyst Complex


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 4.40 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Cryo-EM structure of the exocyst complex

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.

(2018) Nat Struct Mol Biol 25: 139-146

  • DOI: https://doi.org/10.1038/s41594-017-0016-2
  • Primary Citation of Related Structures:  
    5YFP

  • 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.


  • Organizational Affiliation

    Department of Biology, University of Pennsylvania, Philadelphia, PA, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Exocyst complex component SEC31,336Saccharomyces cerevisiae S288CMutation(s): 0 
UniProt
Find proteins for P33332 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore P33332 
Go to UniProtKB:  P33332
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP33332
Sequence Annotations
Expand
  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Exocyst complex component SEC5971Saccharomyces cerevisiae S288CMutation(s): 0 
UniProt
Find proteins for P89102 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore P89102 
Go to UniProtKB:  P89102
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP89102
Sequence Annotations
Expand
  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Exocyst complex component SEC6805Saccharomyces cerevisiae S288CMutation(s): 0 
UniProt
Find proteins for P32844 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore P32844 
Go to UniProtKB:  P32844
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP32844
Sequence Annotations
Expand
  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
Exocyst complex component SEC81,065Saccharomyces cerevisiae S288CMutation(s): 0 
UniProt
Find proteins for P32855 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore P32855 
Go to UniProtKB:  P32855
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP32855
Sequence Annotations
Expand
  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 5
MoleculeChains Sequence LengthOrganismDetailsImage
Exocyst complex component SEC10871Saccharomyces cerevisiae S288CMutation(s): 0 
UniProt
Find proteins for Q06245 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore Q06245 
Go to UniProtKB:  Q06245
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ06245
Sequence Annotations
Expand
  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 6
MoleculeChains Sequence LengthOrganismDetailsImage
Exocyst complex component SEC15910Saccharomyces cerevisiae S288CMutation(s): 0 
UniProt
Find proteins for P22224 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore P22224 
Go to UniProtKB:  P22224
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP22224
Sequence Annotations
Expand
  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 7
MoleculeChains Sequence LengthOrganismDetailsImage
Exocyst complex component EXO70623Saccharomyces cerevisiae S288CMutation(s): 0 
UniProt
Find proteins for P19658 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore P19658 
Go to UniProtKB:  P19658
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP19658
Sequence Annotations
Expand
  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 8
MoleculeChains Sequence LengthOrganismDetailsImage
Exocyst complex component EXO84753Saccharomyces cerevisiae S288CMutation(s): 0 
UniProt
Find proteins for P38261 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore P38261 
Go to UniProtKB:  P38261
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP38261
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 4.40 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 
EM Software:
TaskSoftware PackageVersion
MODEL REFINEMENTPHENIX1.11.1
MODEL REFINEMENTPHENIX1.11.1
MODEL REFINEMENTPHENIX1.11.1
MODEL REFINEMENTCoot0.8.2
MODEL REFINEMENTPHENIX1.11.1
MODEL REFINEMENTPHENIX1.11.1
MODEL REFINEMENTCoot0.8.2
MODEL REFINEMENTPHENIX1.11.1
MODEL REFINEMENTPHENIX1.11.1
RECONSTRUCTIONRELION1.4

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
National Science Foundation of ChinaChina31530018
Beijing Municipal Science & Technology CommissionChinaZ161100000116034
National Key Research and Development Program of MOSTChina2016YFA0501100
National Institute of HealthUnited StatesR01GM111128

Revision History  (Full details and data files)

  • Version 1.0: 2018-01-31
    Type: Initial release
  • Version 1.1: 2018-02-21
    Changes: Database references
  • Version 1.2: 2019-11-06
    Changes: Data collection, Other
  • Version 1.3: 2024-03-27
    Changes: Data collection, Database references, Refinement description