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| Title | Structure of the human BBSome core complex. |
|---|---|
| Journal, issue, pages | Elife, Vol. 9, Year 2020 |
| Publish date | Jan 17, 2020 |
 Authors | Björn Udo Klink / Christos Gatsogiannis / Oliver Hofnagel / Alfred Wittinghofer / Stefan Raunser /  |
| 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 ...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. |
 External links | Elife / PubMed:31951201 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 3.8 - 4.3 Å |
| Structure data | EMDB-10617, PDB-6xt9: EMDB-10618: The human core BBSome complex (BBS 1,4,5,8,9,18) |
| Source |
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 Keywords | PROTEIN TRANSPORT / ciliary transport / Arl6 effector / adaptor protein / complex |
homo sapiens (human)