2FJI

Crystal structure of the C-terminal domain of the exocyst subunit Sec6p

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Free: 0.284 
  • R-Value Work: 0.249 

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This is version 1.4 of the entry. See complete history. 


Literature

The structure of the exocyst subunit Sec6p defines a conserved architecture with diverse roles.

Sivaram, M.V., Furgason, M.L., Brewer, D.N., Munson, M.

(2006) Nat Struct Mol Biol 13: 555-556

  • DOI: https://doi.org/10.1038/nsmb1096
  • Primary Citation of Related Structures:  
    2FJI

  • PubMed Abstract: 

    The exocyst is a conserved protein complex essential for trafficking secretory vesicles to the plasma membrane. The structure of the C-terminal domain of the exocyst subunit Sec6p reveals multiple helical bundles, which are structurally and topologically similar to Exo70p and the C-terminal domains of Exo84p and Sec15, despite <10% sequence identity. The helical bundles appear to be evolutionarily related molecular scaffolds that have diverged to create functionally distinct exocyst proteins.

    • Organizational Affiliation: 

    Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, 364 Plantation Street, Worcester, Massachusetts 01605, USA.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Exocyst complex component SEC6A [auth 1],
B [auth 2]		399Saccharomyces cerevisiaeMutation(s): 0 
Gene Names: SEC6
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
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Free: 0.284 
  • R-Value Work: 0.249 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 108.295α = 90
b = 63.301β = 103.89
c = 151.468γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
SHARPphasing
CNSrefinement
PDB_EXTRACTdata extraction
HKL-2000data reduction

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2006-05-16
    Type: Initial release
  • Version 1.1: 2008-05-01
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2017-10-18
    Changes: Advisory, Refinement description
  • Version 1.4: 2024-02-14
    Changes: Advisory, Data collection, Database references