6VBV
Structure of the bovine BBSome:ARL6:GTP complex
Summary for 6VBV
| Entry DOI | 10.2210/pdb6vbv/pdb |
| EMDB information | 21145 |
| Descriptor | Bardet-Biedl syndrome 18 protein, CALCIUM ION, GUANOSINE-5'-TRIPHOSPHATE, ... (11 entities in total) |
| Functional Keywords | cilia, ciliopathy, complex, membrane-protein transport, protein transport |
| Biological source | Bos taurus (Bovine) More |
| Total number of polymer chains | 9 |
| Total formula weight | 508169.76 |
| Authors | Singh, S.K.,Gui, M.,Koh, F.,Yip, M.C.J.,Brown, A. (deposition date: 2019-12-19, release date: 2020-01-29, Last modification date: 2024-03-06) |
| Primary citation | Singh, S.K.,Gui, M.,Koh, F.,Yip, M.C.,Brown, A. Structure and activation mechanism of the BBSome membrane protein trafficking complex. Elife, 9:-, 2020 Cited by 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. PubMed: 31939736DOI: 10.7554/eLife.53322 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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