4GKW

Crystal Structure of the Coiled-coil Domain of C. elegans SAS-6


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.30 Å
  • R-Value Free: 0.299 
  • R-Value Work: 0.258 
  • R-Value Observed: 0.270 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

SAS-6 coiled-coil structure and interaction with SAS-5 suggest a regulatory mechanism in C. elegans centriole assembly.

Qiao, R.Cabral, G.Lettman, M.M.Dammermann, A.Dong, G.

(2012) EMBO J 31: 4334-4347

  • DOI: https://doi.org/10.1038/emboj.2012.280
  • Primary Citation of Related Structures:  
    4GKW

  • PubMed Abstract: 

    The centriole is a conserved microtubule-based organelle essential for both centrosome formation and cilium biogenesis. Five conserved proteins for centriole duplication have been identified. Two of them, SAS-5 and SAS-6, physically interact with each other and are codependent for their targeting to procentrioles. However, it remains unclear how these two proteins interact at the molecular level. Here, we demonstrate that the short SAS-5 C-terminal domain (residues 390-404) specifically binds to a narrow central region (residues 275-288) of the SAS-6 coiled coil. This was supported by the crystal structure of the SAS-6 coiled-coil domain (CCD), which, together with mutagenesis studies, indicated that the association is mediated by synergistic hydrophobic and electrostatic interactions. The crystal structure also shows a periodic charge pattern along the SAS-6 CCD, which gives rise to an anti-parallel tetramer. Overall, our findings establish the molecular basis of the specific interaction between SAS-5 and SAS-6, and suggest that both proteins individually adopt an oligomeric conformation that is disrupted upon the formation of the hetero-complex to facilitate the correct assembly of the nine-fold symmetric centriole.


  • Organizational Affiliation

    Max F Perutz Laboratories, Medical University of Vienna, Vienna, Austria.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Spindle assembly abnormal protein 6
A, B
167Caenorhabditis elegansMutation(s): 0 
Gene Names: sas-6Y45F10D.9
UniProt
Find proteins for O62479 (Caenorhabditis elegans)
Explore O62479 
Go to UniProtKB:  O62479
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO62479
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.30 Å
  • R-Value Free: 0.299 
  • R-Value Work: 0.258 
  • R-Value Observed: 0.270 
  • Space Group: P 61
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 140.29α = 90
b = 140.29β = 90
c = 74.67γ = 120
Software Package:
Software NamePurpose
ADSCdata collection
SHELXSphasing
CNSrefinement
MOSFLMdata reduction
SCALAdata scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2012-11-21
    Type: Initial release
  • Version 1.1: 2012-11-28
    Changes: Database references
  • Version 1.2: 2024-02-28
    Changes: Data collection, Database references