8bda
From Proteopedia
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| - | ==IFTA complex in anterograde | + | ==IFTA complex in anterograde intraflagellar transport trains (Chlamydomonas reinhardtii)== |
<StructureSection load='8bda' size='340' side='right'caption='[[8bda]], [[Resolution|resolution]] 20.70Å' scene=''> | <StructureSection load='8bda' size='340' side='right'caption='[[8bda]], [[Resolution|resolution]] 20.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8bda]] is a 5 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=8BDA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BDA FirstGlance]. <br> | <table><tr><td colspan='2'>[[8bda]] is a 5 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=8BDA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BDA FirstGlance]. <br> | ||
| - | </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=8bda FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bda OCA], [https://pdbe.org/8bda PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bda RCSB], [https://www.ebi.ac.uk/pdbsum/8bda PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bda ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 20.7Å</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=8bda FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bda OCA], [https://pdbe.org/8bda PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bda RCSB], [https://www.ebi.ac.uk/pdbsum/8bda PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bda ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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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. | 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. | ||
| - | 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 | + | 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 May;30(5):584-593. doi: 10.1038/s41594-022-00905-5. , Epub 2023 Jan 2. PMID:36593313<ref>PMID:36593313</ref> |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
Current revision
IFTA complex in anterograde intraflagellar transport trains (Chlamydomonas reinhardtii)
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