View source for 6kio


==Complex of yeast cytoplasmic dynein MTBD-High and MT without DTT==
<SX load='6kio' size='340' side='right' viewer='molstar' caption='[[6kio]], [[Resolution|resolution]] 3.94&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6kio]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C] and [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KIO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KIO FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.94&#8491;</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=6kio FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kio OCA], [https://pdbe.org/6kio PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6kio RCSB], [https://www.ebi.ac.uk/pdbsum/6kio PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6kio ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TBB_PIG TBB_PIG] 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.
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== Publication Abstract from PubMed ==
The movements of cytoplasmic dynein on microtubule (MT) tracks is achieved by two-way communication between the microtubule-binding domain (MTBD) and the ATPase domain via a coiled-coil stalk, but the structural basis of this communication remains elusive. Here, we regulate MTBD either in high-affinity or low-affinity states by introducing a disulfide bond to the stalk and analyze the resulting structures by NMR and cryo-EM. In the MT-unbound state, the affinity changes of MTBD are achieved by sliding of the stalk alpha-helix by a half-turn, which suggests that structural changes propagate from the ATPase-domain to MTBD. In addition, MT binding induces further sliding of the stalk alpha-helix even without the disulfide bond, suggesting how the MT-induced conformational changes propagate toward the ATPase domain. Based on differences in the MT-binding surface between the high- and low-affinity states, we propose a potential mechanism for the directional bias of dynein movement on MT tracks.

Structural basis for two-way communication between dynein and microtubules.,Nishida N, Komori Y, Takarada O, Watanabe A, Tamura S, Kubo S, Shimada I, Kikkawa M Nat Commun. 2020 Feb 25;11(1):1038. doi: 10.1038/s41467-020-14842-8. PMID:32098965<ref>PMID:32098965</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6kio" style="background-color:#fffaf0;"></div>

==See Also==
*[[Dynein 3D structures|Dynein 3D structures]]
*[[Tubulin 3D Structures|Tubulin 3D Structures]]
== References ==
<references/>
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Sus scrofa]]
[[Category: Kikkawa M]]
[[Category: Komori Y]]
[[Category: Nishida N]]
[[Category: Shimada I]]