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TitleThe Molecular Architecture of Native BBSome Obtained by an Integrated Structural Approach.
Journal, issue, pagesStructure, Vol. 27, Issue 9, Page 1384-11394.e4, Year 2019
Publish dateSep 3, 2019
AuthorsHui-Ting Chou / Luise Apelt / Daniel P Farrell / Susan Roehl White / Jonathan Woodsmith / Vladimir Svetlov / Jaclyn S Goldstein / Andrew R Nager / Zixuan Li / Jean Muller / Hélène Dollfus / Evgeny Nudler / Ulrich Stelzl / Frank DiMaio / Maxence V Nachury / Thomas Walz /
PubMed AbstractThe unique membrane composition of cilia is maintained by a diffusion barrier at the transition zone that is breached when the BBSome escorts signaling receptors out of cilia. Understanding how the ...The unique membrane composition of cilia is maintained by a diffusion barrier at the transition zone that is breached when the BBSome escorts signaling receptors out of cilia. Understanding how the BBSome removes proteins from cilia has been hampered by a lack of structural information. Here, we present a nearly complete Cα model of BBSome purified from cow retina. The model is based on a single-particle cryo-electron microscopy density map at 4.9-Å resolution that was interpreted with the help of comprehensive Rosetta-based structural modeling constrained by crosslinking mass spectrometry data. We find that BBSome subunits have a very high degree of interconnectivity, explaining the obligate nature of the complex. Furthermore, like other coat adaptors, the BBSome exists in an autoinhibited state in solution and must thus undergo a conformational change upon recruitment to membranes by the small GTPase ARL6/BBS3. Our model provides the first detailed view of the machinery enabling ciliary exit.
External linksStructure / PubMed:31303482 / PubMed Central
MethodsEM (single particle)
Resolution4.9 - 7.0 Å
Structure data

EMDB-7839:
BBSome complex
Method: EM (single particle) / Resolution: 4.9 Å

EMDB-7841:
BBSome subcomplex
Method: EM (single particle) / Resolution: 7.0 Å

Source
  • Bos taurus (cattle)

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