4YV4

Structure of the C. elegans SAS-5 coiled coil domain


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.239 
  • R-Value Work: 0.211 
  • R-Value Observed: 0.212 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

The Caenorhabditis elegans protein SAS-5 forms large oligomeric assemblies critical for centriole formation.

Rogala, K.B.Dynes, N.J.Hatzopoulos, G.N.Yan, J.Pong, S.K.Robinson, C.V.Deane, C.M.Gonczy, P.Vakonakis, I.

(2015) Elife 4: e07410-e07410

  • DOI: https://doi.org/10.7554/eLife.07410
  • Primary Citation of Related Structures:  
    4YNH, 4YV4

  • PubMed Abstract: 

    Centrioles are microtubule-based organelles crucial for cell division, sensing and motility. In Caenorhabditis elegans, the onset of centriole formation requires notably the proteins SAS-5 and SAS-6, which have functional equivalents across eukaryotic evolution. Whereas the molecular architecture of SAS-6 and its role in initiating centriole formation are well understood, the mechanisms by which SAS-5 and its relatives function is unclear. Here, we combine biophysical and structural analysis to uncover the architecture of SAS-5 and examine its functional implications in vivo. Our work reveals that two distinct self-associating domains are necessary to form higher-order oligomers of SAS-5: a trimeric coiled coil and a novel globular dimeric Implico domain. Disruption of either domain leads to centriole duplication failure in worm embryos, indicating that large SAS-5 assemblies are necessary for function in vivo.


  • Organizational Affiliation

    Department of Biochemistry, University of Oxford, Oxford, United Kingdom.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Spindle assembly abnormal protein 5
A, B, C, D, E
A, B, C, D, E, F, G, H
58Caenorhabditis elegansMutation(s): 0 
Gene Names: sas-5F35B12.5
UniProt
Find proteins for Q20010 (Caenorhabditis elegans)
Explore Q20010 
Go to UniProtKB:  Q20010
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ20010
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.239 
  • R-Value Work: 0.211 
  • R-Value Observed: 0.212 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 46.6α = 90
b = 55.07β = 90
c = 191.53γ = 90
Software Package:
Software NamePurpose
BUSTERrefinement
XDSdata reduction
XSCALEdata scaling
PHENIXphasing

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Biotechnology and Biological Sciences Research CouncilUnited KingdomBB/J008265/1
Wellcome TrustUnited Kingdom088497/Z/09/Z

Revision History  (Full details and data files)

  • Version 1.0: 2015-06-10
    Type: Initial release
  • Version 1.1: 2015-08-26
    Changes: Database references
  • Version 1.2: 2017-08-30
    Changes: Author supporting evidence
  • Version 1.3: 2024-05-08
    Changes: Data collection, Database references