6XTB
Subunit BBS 5 of the human core BBSome complex
Summary for 6XTB
| Entry DOI | 10.2210/pdb6xtb/pdb |
| Related | 6XT9 |
| EMDB information | 10617 10618 |
| Descriptor | Bardet-Biedl syndrome 5 protein (1 entity in total) |
| Functional Keywords | ciliary transport, arl6 effector, adaptor protein, complex, protein transport |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 38797.93 |
| Authors | Klink, B.U.,Raunser, S.,Gatsogiannis, C. (deposition date: 2020-01-15, release date: 2020-02-19, Last modification date: 2024-05-22) |
| Primary citation | Klink, B.U.,Gatsogiannis, C.,Hofnagel, O.,Wittinghofer, A.,Raunser, S. Structure of the human BBSome core complex. Elife, 9:-, 2020 Cited by PubMed Abstract: The BBSome is a heterooctameric protein complex that plays a central role in primary cilia homeostasis. Its malfunction causes the severe ciliopathy Bardet-Biedl syndrome (BBS). The complex acts as a cargo adapter that recognizes signaling proteins such as GPCRs and links them to the intraflagellar transport machinery. The underlying mechanism is poorly understood. Here we present a high-resolution cryo-EM structure of a human heterohexameric core subcomplex of the BBSome. The structure reveals the architecture of the complex in atomic detail. It explains how the subunits interact with each other and how disease-causing mutations hamper this interaction. The complex adopts a conformation that is open for binding to membrane-associated GTPase Arl6 and a large positively charged patch likely strengthens the interaction with the membrane. A prominent negatively charged cleft at the center of the complex is likely involved in binding of positively charged signaling sequences of cargo proteins. PubMed: 31951201DOI: 10.7554/eLife.53910 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.3 Å) |
Structure validation
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