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==Cryo-EM structure of microtubule-bound KLP61F motor with tail domain in the nucleotide-free state==
==Cryo-EM structure of microtubule-bound KLP61F motor with tail domain in the nucleotide-free state==
<StructureSection load='6vpp' size='340' side='right'caption='[[6vpp]], [[Resolution|resolution]] 4.40&Aring;' scene=''>
<SX load='6vpp' size='340' side='right' viewer='molstar' caption='[[6vpp]], [[Resolution|resolution]] 4.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6vpp]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VPP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6VPP FirstGlance]. <br>
<table><tr><td colspan='2'>[[6vpp]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] 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=6VPP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VPP FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 4.4&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6vpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vpp OCA], [http://pdbe.org/6vpp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vpp RCSB], [http://www.ebi.ac.uk/pdbsum/6vpp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vpp 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></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=6vpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vpp OCA], [https://pdbe.org/6vpp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vpp RCSB], [https://www.ebi.ac.uk/pdbsum/6vpp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vpp ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/TBA1A_PIG TBA1A_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. [[http://www.uniprot.org/uniprot/KL61_DROME KL61_DROME]] Important role in mitotic dividing cells. Microtubule motor required for spindle body separation. Slow plus-end directed microtubule motor capable of cross-linking and sliding apart antiparallel microtubules, thereby pushing apart the associated spindle poles during spindle assembly and function. [[http://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.
[https://www.uniprot.org/uniprot/TBA1A_PIG TBA1A_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.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Kinesin-5 motors organize mitotic spindles by sliding apart microtubules. They are homotetramers with dimeric motor and tail domains at both ends of a bipolar minifilament. Here, we describe a regulatory mechanism involving direct binding between tail and motor domains and its fundamental role in microtubule sliding. Kinesin-5 tails decrease microtubule-stimulated ATP-hydrolysis by specifically engaging motor domains in the nucleotide-free or ADP states. Cryo-EM reveals that tail binding stabilizes an open motor domain ATP-active site. Full-length motors undergo slow motility and cluster together along microtubules, while tail-deleted motors exhibit rapid motility without clustering. The tail is critical for motors to zipper together two microtubules by generating substantial sliding forces. The tail is essential for mitotic spindle localization, which becomes severely reduced in tail-deleted motors. Our studies suggest a revised microtubule-sliding model, in which kinesin-5 tails stabilize motor domains in the microtubule-bound state by slowing ATP-binding, resulting in high-force production at both homotetramer ends.


The kinesin-5 tail domain directly modulates the mechanochemical cycle of the motor domain for anti-parallel microtubule sliding.,Bodrug T, Wilson-Kubalek EM, Nithianantham S, Thompson AF, Alfieri A, Gaska I, Major J, Debs G, Inagaki S, Gutierrez P, Gheber L, McKenney RJ, Sindelar CV, Milligan R, Stumpff J, Rosenfeld SS, Forth ST, Al-Bassam J Elife. 2020 Jan 20;9. pii: 51131. doi: 10.7554/eLife.51131. PMID:31958056<ref>PMID:31958056</ref>
==See Also==
 
*[[Kinesin 3D Structures|Kinesin 3D Structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
*[[Tubulin 3D Structures|Tubulin 3D Structures]]
</div>
<div class="pdbe-citations 6vpp" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</SX>
[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
[[Category: Al-Bassam, J]]
[[Category: Al-Bassam J]]
[[Category: Bodrug, T]]
[[Category: Bodrug T]]
[[Category: Debs, G]]
[[Category: Debs G]]
[[Category: Milligan, R]]
[[Category: Milligan R]]
[[Category: Nithianantham, S]]
[[Category: Nithianantham S]]
[[Category: Sindelar, C V]]
[[Category: Sindelar CV]]
[[Category: Wilson-Kubalek, E M]]
[[Category: Wilson-Kubalek EM]]
[[Category: Cell cycle]]
[[Category: Kinesin-5]]
[[Category: Klp61f]]
[[Category: Microtubule]]
[[Category: Mitotic spindle]]
[[Category: Motor protein]]
[[Category: Nucleotide-free state]]

Latest revision as of 17:39, 6 March 2024

Cryo-EM structure of microtubule-bound KLP61F motor with tail domain in the nucleotide-free stateCryo-EM structure of microtubule-bound KLP61F motor with tail domain in the nucleotide-free state

6vpp, resolution 4.40Å

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