6XT9

Subunits BBS 1,4,8,9,18 of the human BBSome complex

Summary for 6XT9

• Entry DOI: 10.2210/pdb6xt9/pdb
• EMDB information: 10617 10618
• Descriptor: Bardet-Biedl syndrome 1 protein, Bardet-Biedl syndrome 4 protein, Tetratricopeptide repeat domain 8 isoform 2, ... (5 entities in total)
• Functional Keywords: ciliary transport, arl6 effector, adaptor protein, complex, protein transport
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 5
• Total formula weight: 298139.56

Authors

Klink, B.U.,Raunser, S.,Gatsogiannis, C. (deposition date: 2020-01-15, release date: 2020-01-29, 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

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: 31951201
DOI: 10.7554/eLife.53910

Experimental method

ELECTRON MICROSCOPY (3.8 Å)