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TitleStructure and activation mechanism of the BBSome membrane protein trafficking complex.
Journal, issue, pagesElife, Vol. 9, Year 2020
Publish dateJan 15, 2020
AuthorsSandeep K Singh / Miao Gui / Fujiet Koh / Matthew Cj Yip / Alan Brown /
PubMed AbstractBardet-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 ...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.
External linksElife / PubMed:31939736 / PubMed Central
MethodsEM (single particle)
Resolution3.1 - 3.5 Å
Structure data

21144

6vbu

EMDB-21144, PDB-6vbu:
Structure of the bovine BBSome complex
Method: EM (single particle) / Resolution: 3.1 Å

21145

6vbv

EMDB-21145, PDB-6vbv:
Structure of the bovine BBSome:ARL6:GTP complex
Method: EM (single particle) / Resolution: 3.5 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM

Source
  • bos taurus (domestic cattle)
KeywordsPROTEIN TRANSPORT / Cilia / ciliopathy / complex / membrane-protein transport

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