8bd7

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'''Unreleased structure'''
 
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The entry 8bd7 is ON HOLD until Paper Publication
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==IFTB1 subcomplex of anterograde Intraflagellar transport trains (Chlamydomonas reinhardtii)==
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<StructureSection load='8bd7' size='340' side='right'caption='[[8bd7]], [[Resolution|resolution]] 9.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8bd7]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8BD7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BD7 FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8bd7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bd7 OCA], [https://pdbe.org/8bd7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bd7 RCSB], [https://www.ebi.ac.uk/pdbsum/8bd7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bd7 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A8JCJ2_CHLRE A8JCJ2_CHLRE]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Anterograde intraflagellar transport (IFT) trains are essential for cilia assembly and maintenance. These trains are formed of 22 IFT-A and IFT-B proteins that link structural and signaling cargos to microtubule motors for import into cilia. It remains unknown how the IFT-A/-B proteins are arranged into complexes and how these complexes polymerize into functional trains. Here we use in situ cryo-electron tomography of Chlamydomonas reinhardtii cilia and AlphaFold2 protein structure predictions to generate a molecular model of the entire anterograde train. We show how the conformations of both IFT-A and IFT-B are dependent on lateral interactions with neighboring repeats, suggesting that polymerization is required to cooperatively stabilize the complexes. Following three-dimensional classification, we reveal how IFT-B extends two flexible tethers to maintain a connection with IFT-A that can withstand the mechanical stresses present in actively beating cilia. Overall, our findings provide a framework for understanding the fundamental processes that govern cilia assembly.
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Authors:
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The molecular structure of IFT-A and IFT-B in anterograde intraflagellar transport trains.,Lacey SE, Foster HE, Pigino G Nat Struct Mol Biol. 2023 Jan 2. doi: 10.1038/s41594-022-00905-5. PMID:36593313<ref>PMID:36593313</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 8bd7" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Chlamydomonas reinhardtii]]
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[[Category: Large Structures]]
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[[Category: Foster HE]]
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[[Category: Lacey SE]]
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[[Category: Pigino G]]

Revision as of 07:39, 11 January 2023

IFTB1 subcomplex of anterograde Intraflagellar transport trains (Chlamydomonas reinhardtii)

PDB ID 8bd7

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