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| | <SX load='6u42' size='340' side='right' viewer='molstar' caption='[[6u42]], [[Resolution|resolution]] 3.40Å' scene=''> | | <SX load='6u42' size='340' side='right' viewer='molstar' caption='[[6u42]], [[Resolution|resolution]] 3.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6u42]] is a 451 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=6U42 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6U42 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6u42]] is a 35 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=6U42 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6U42 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></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]] 3.4Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nucleoside-diphosphate_kinase Nucleoside-diphosphate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.6 2.7.4.6] </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></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=6u42 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6u42 OCA], [http://pdbe.org/6u42 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6u42 RCSB], [http://www.ebi.ac.uk/pdbsum/6u42 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6u42 ProSAT]</span></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=6u42 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6u42 OCA], [https://pdbe.org/6u42 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6u42 RCSB], [https://www.ebi.ac.uk/pdbsum/6u42 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6u42 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/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. [[http://www.uniprot.org/uniprot/ODA1_CHLRE ODA1_CHLRE]] Component of the outer dynein arm complex required for assembly of the outer dynein arm-docking complex (ODA-DC) and the outer dynein arm onto the doublet microtubule.<ref>PMID:11907279</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/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/CFA53_CHLRE CFA53_CHLRE]] May play a role in filopodium movement.[UniProtKB:Q96M91] | + | [https://www.uniprot.org/uniprot/A8IY81_CHLRE A8IY81_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 6u42" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6u42" 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: Nucleoside-diphosphate kinase]]
| + | [[Category: Brown A]] |
| - | [[Category: Brown, A]] | + | [[Category: Dutcher SK]] |
| - | [[Category: Dutcher, S K]] | + | [[Category: Ma M]] |
| - | [[Category: Ma, M]] | + | [[Category: Rademacher G]] |
| - | [[Category: Rademacher, G]] | + | [[Category: Stoyanova M]] |
| - | [[Category: Stoyanova, M]] | + | [[Category: Zhang R]] |
| - | [[Category: Zhang, R]] | + | |
| - | [[Category: Microtubule doublet]]
| + | |
| - | [[Category: Motile cilia]]
| + | |
| - | [[Category: Protein fibril]]
| + | |
| - | [[Category: Repetitive structure]]
| + | |
| Structural highlights
Function
A8IY81_CHLRE
Publication Abstract from PubMed
The axoneme of motile cilia is the largest macromolecular machine of eukaryotic cells. In humans, impaired axoneme function causes a range of ciliopathies. Axoneme assembly, structure, and motility require a radially arranged set of doublet microtubules, each decorated in repeating patterns with non-tubulin components. We use single-particle cryo-electron microscopy to visualize and build an atomic model of the repeating structure of a native axonemal doublet microtubule, which reveals the identities, positions, repeat lengths, and interactions of 38 associated proteins, including 33 microtubule inner proteins (MIPs). The structure demonstrates how these proteins establish the unique architecture of doublet microtubules, maintain coherent periodicities along the axoneme, and stabilize the microtubules against the repeated mechanical stress induced by ciliary motility. Our work elucidates the architectural principles that underpin the assembly of this large, repetitive eukaryotic structure and provides a molecular basis for understanding the etiology of human ciliopathies.
Structure of the Decorated Ciliary Doublet Microtubule.,Ma M, Stoyanova M, Rademacher G, Dutcher SK, Brown A, Zhang R Cell. 2019 Oct 31;179(4):909-922.e12. doi: 10.1016/j.cell.2019.09.030. Epub 2019 , Oct 24. PMID:31668805[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ma M, Stoyanova M, Rademacher G, Dutcher SK, Brown A, Zhang R. Structure of the Decorated Ciliary Doublet Microtubule. Cell. 2019 Oct 31;179(4):909-922.e12. doi: 10.1016/j.cell.2019.09.030. Epub 2019 , Oct 24. PMID:31668805 doi:http://dx.doi.org/10.1016/j.cell.2019.09.030
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