6vbu
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the bovine BBSome complex== | |
| + | <StructureSection load='6vbu' size='340' side='right'caption='[[6vbu]], [[Resolution|resolution]] 3.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6vbu]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VBU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6VBU FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6vbu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vbu OCA], [http://pdbe.org/6vbu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vbu RCSB], [http://www.ebi.ac.uk/pdbsum/6vbu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vbu ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/F1MB52_BOVIN F1MB52_BOVIN]] The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function.[PIRNR:PIRNR011091] [[http://www.uniprot.org/uniprot/BBS4_BOVIN BBS4_BOVIN]] May be required for the dynein-mediated transport of pericentriolar proteins to the centrosome. Required for microtubule anchoring at the centrosome but not for microtubule nucleation. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of the ciliary membrane (By similarity). [[http://www.uniprot.org/uniprot/A6QLF9_BOVIN A6QLF9_BOVIN]] The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of the ciliary membrane. The BBSome complex, together with the LTZL1, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation. Required for BBSome complex ciliary localization but not for the proper complex assembly.[PIRNR:PIRNR010072] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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 A 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 b-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. | ||
| - | + | Structure and activation mechanism of the BBSome membrane protein trafficking complex.,Singh SK, Gui M, Koh F, Yip MC, Brown A Elife. 2020 Jan 15;9. pii: 53322. doi: 10.7554/eLife.53322. PMID:31939736<ref>PMID:31939736</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6vbu" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bos taurus]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Brown, A]] | [[Category: Brown, A]] | ||
| - | [[Category: Yip, M.C.J]] | ||
[[Category: Gui, M]] | [[Category: Gui, M]] | ||
[[Category: Koh, F]] | [[Category: Koh, F]] | ||
| - | [[Category: Singh, S | + | [[Category: Singh, S K]] |
| + | [[Category: Yip, M C.J]] | ||
| + | [[Category: Cilia]] | ||
| + | [[Category: Ciliopathy]] | ||
| + | [[Category: Complex]] | ||
| + | [[Category: Membrane-protein transport]] | ||
| + | [[Category: Protein transport]] | ||
Revision as of 15:47, 29 January 2020
Structure of the bovine BBSome complex
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