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| | <SX load='6ve7' size='340' side='right' viewer='molstar' caption='[[6ve7]], [[Resolution|resolution]] 3.60Å' scene=''> | | <SX load='6ve7' size='340' side='right' viewer='molstar' caption='[[6ve7]], [[Resolution|resolution]] 3.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6ve7]] is a 62 chain structure with sequence from [http://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VE7 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6VE7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6ve7]] is a 62 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=6VE7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VE7 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TA1:TAXOL'>TA1</scene></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]] 3.6Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6ve7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ve7 OCA], [http://pdbe.org/6ve7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ve7 RCSB], [http://www.ebi.ac.uk/pdbsum/6ve7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ve7 ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TA1:TAXOL'>TA1</scene></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=6ve7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ve7 OCA], [https://pdbe.org/6ve7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ve7 RCSB], [https://www.ebi.ac.uk/pdbsum/6ve7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ve7 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TBA1_CHLRE TBA1_CHLRE]] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. [[http://www.uniprot.org/uniprot/CFA20_CHLRE CFA20_CHLRE]] Cilium- and flagellum-specific protein that plays a role in axonemal structure organization and motility (PubMed:24259666, PubMed:24574454). Involved in the control of flagellar beating in an asymmetric and planar waveform (PubMed:24259666, PubMed:24574454). Stabilizes outer doublet microtubules (DMTs) of the axoneme and may work as a scaffold for intratubular proteins, such as tektin and PACRG, to produce the beak structures in DMT1, 5 and 6 (PubMed:24259666, PubMed:24574454). Not essential for flagellar assembly (PubMed:24574454).<ref>PMID:24259666</ref> <ref>PMID:24574454</ref> [[http://www.uniprot.org/uniprot/FLTOP_CHLRE FLTOP_CHLRE]] May act as a regulator of cilium basal body docking and positioning in mono- and multiciliated cells.[UniProtKB:Q6P8X9] [[http://www.uniprot.org/uniprot/TBB_CHLRE TBB_CHLRE]] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. | + | [https://www.uniprot.org/uniprot/A8J098_CHLRE A8J098_CHLRE] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6ve7" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6ve7" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Tubulin 3D Structures|Tubulin 3D Structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | [[Category: Chlamydomonas reinhardtii]] | | [[Category: Chlamydomonas reinhardtii]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bui, K H]] | + | [[Category: Bui KH]] |
| - | [[Category: Ichikawa, M]] | + | [[Category: Ichikawa M]] |
| - | [[Category: Khalifa, A A.Z]] | + | [[Category: Khalifa AAZ]] |
| - | [[Category: Axoneme]]
| + | |
| - | [[Category: Cilia]]
| + | |
| - | [[Category: Doublet]]
| + | |
| - | [[Category: Microtubule inner protein]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| Structural highlights
Function
A8J098_CHLRE
Publication Abstract from PubMed
Microtubules are cytoskeletal structures involved in stability, transport and organization in the cell. The building blocks, the alpha- and beta-tubulin heterodimers, form protofilaments that associate laterally into the hollow microtubule. Microtubule also exists as highly stable doublet microtubules in the cilia where stability is needed for ciliary beating and function. The doublet microtubule maintains its stability through interactions at its inner and outer junctions where its A- and B-tubules meet. Here, using cryo-electron microscopy, bioinformatics and mass spectrometry of the doublets of Chlamydomonas reinhardtii and Tetrahymena thermophila, we identified two new inner junction proteins, FAP276 and FAP106, and an inner junction-associated protein, FAP126, thus presenting the complete answer to the inner junction identity and localization. Our structural study of the doublets shows that the inner junction serves as an interaction hub that involves tubulin post-translational modifications. These interactions contribute to the stability of the doublet and hence, normal ciliary motility.
The inner junction complex of the cilia is an interaction hub that involves tubulin post-translational modifications.,Khalifa AAZ, Ichikawa M, Dai D, Kubo S, Black CS, Peri K, McAlear TS, Veyron S, Yang SK, Vargas J, Bechstedt S, Trempe JF, Bui KH Elife. 2020 Jan 17;9. pii: 52760. doi: 10.7554/eLife.52760. PMID:31951202[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Khalifa AAZ, Ichikawa M, Dai D, Kubo S, Black CS, Peri K, McAlear TS, Veyron S, Yang SK, Vargas J, Bechstedt S, Trempe JF, Bui KH. The inner junction complex of the cilia is an interaction hub that involves tubulin post-translational modifications. Elife. 2020 Jan 17;9. pii: 52760. doi: 10.7554/eLife.52760. PMID:31951202 doi:http://dx.doi.org/10.7554/eLife.52760
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