6VBV

Structure of the bovine BBSome:ARL6:GTP complex


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.50 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


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Literature

Structure and activation mechanism of the BBSome membrane protein trafficking complex.

Singh, S.K.Gui, M.Koh, F.Yip, M.C.Brown, A.

(2020) Elife 9

  • DOI: https://doi.org/10.7554/eLife.53322
  • Primary Citation of Related Structures:  
    6VBU, 6VBV

  • PubMed Abstract: 

    Bardet-Biedl syndrome (BBS) is a currently incurable ciliopathy caused by the failure to correctly establish or maintain cilia-dependent signaling pathways. Eight proteins associated with BBS assemble into the BBSome, a key regulator of the ciliary membrane proteome. We report the electron cryomicroscopy (cryo-EM) structures of the native bovine BBSome in inactive and active states at 3.1 and 3.5 Å resolution, respectively. In the active state, the BBSome is bound to an Arf-family GTPase (ARL6/BBS3) that recruits the BBSome to ciliary membranes. ARL6 recognizes a composite binding site formed by BBS1 and BBS7 that is occluded in the inactive state. Activation requires an unexpected swiveling of the β-propeller domain of BBS1, the subunit most frequently implicated in substrate recognition, which widens a central cavity of the BBSome. Structural mapping of disease-causing mutations suggests that pathogenesis results from folding defects and the disruption of autoinhibition and activation.


  • Organizational Affiliation

    Department of Biological Chemistry and Molecular Pharmacology, Blavatnik Institute, Harvard Medical School, Boston, United States.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Bardet-Biedl syndrome 18 proteinA [auth 0]69Bos taurusMutation(s): 0 
UniProt
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UniProt GroupG3N2W1
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
BBS1 domain-containing proteinB [auth 1]592Bos taurusMutation(s): 0 
UniProt
Find proteins for E1BN34 (Bos taurus)
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Bardet-Biedl syndrome 2 protein homologC [auth 2]721Bos taurusMutation(s): 0 
UniProt
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
Bardet-Biedl syndrome 4 protein homologD [auth 4]519Bos taurusMutation(s): 0 
UniProt
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Entity ID: 5
MoleculeChains Sequence LengthOrganismDetailsImage
Bardet-Biedl syndrome 5 protein homologE [auth 5]341Bos taurusMutation(s): 0 
UniProt
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Entity ID: 6
MoleculeChains Sequence LengthOrganismDetailsImage
Bardet-Biedl syndrome 7 protein homologF [auth 7]715Bos taurusMutation(s): 0 
UniProt
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UniProt GroupF1MB52
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Entity ID: 7
MoleculeChains Sequence LengthOrganismDetailsImage
Tetratricopeptide repeat domain 8G [auth 8]501Bos taurusMutation(s): 0 
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Entity ID: 8
MoleculeChains Sequence LengthOrganismDetailsImage
Bardet-Biedl syndrome 9H [auth 9]887Bos taurusMutation(s): 0 
UniProt
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Entity ID: 9
MoleculeChains Sequence LengthOrganismDetailsImage
ADP-ribosylation factor-like protein 6I [auth 3]186Bos taurusMutation(s): 0 
Gene Names: ARL6
UniProt
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Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.50 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 
EM Software:
TaskSoftware PackageVersion
RECONSTRUCTIONRELION3.0
MODEL REFINEMENTPHENIX1.17.1-3660

Structure Validation

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Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Other privateUnited States--

Revision History  (Full details and data files)

  • Version 1.0: 2020-01-29
    Type: Initial release
  • Version 1.1: 2024-03-06
    Changes: Data collection, Database references