View source for 2wbe

==Kinesin-5-Tubulin Complex with AMPPNP==
<StructureSection load='2wbe' size='340' side='right' caption='[[2wbe]], [[Resolution|resolution]] 9.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2wbe]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WBE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WBE FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1z2b|1z2b]], [[1sa1|1sa1]], [[1sa0|1sa0]], [[1jff|1jff]], [[1tvk|1tvk]]</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=2wbe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wbe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wbe RCSB], [http://www.ebi.ac.uk/pdbsum/2wbe PDBsum]</span></td></tr>
</table>
== 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. 
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wb/2wbe_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Kinesin-5 (K5) motors are important components of the microtubule (MT)-based cell division machinery and are targets for small-molecule inhibitors currently in cancer clinical trials. However, the nature of the K5-MT interaction and the regulatory mechanisms that control it remain unclear. Using cryo-electron microscopy and image processing, we calculated the structure of a K5 motor bound to MTs at 9 A resolution, providing insight into this important interaction. Our reconstruction reveals the K5 motor domain in an ATP-like conformation in which MT binding induces the conserved nucleotide-sensing switch I and II loops to form a compact subdomain around the bound nucleotide. Our reconstruction also reveals a novel conformation for the K5-specific drug-binding loop 5, suggesting a possible role for it in switching K5s between force generation and diffusional modes of MT binding. Our data thus shed light on regulation of the interaction between spindle components important for chromosome segregation.

9-Angstrom structure of a microtubule-bound mitotic motor.,Bodey AJ, Kikkawa M, Moores CA J Mol Biol. 2009 May 1;388(2):218-24. Epub 2009 Mar 10. PMID:19285086<ref>PMID:19285086</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>

==See Also==
*[[Kinesin|Kinesin]]
*[[Tubulin|Tubulin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bos taurus]]
[[Category: Drosophila melanogaster]]
[[Category: Bodey, A J]]
[[Category: Kikkawa, M]]
[[Category: Moores, C A]]
[[Category: Atp-binding]]
[[Category: Cell cycle]]
[[Category: Cell division]]
[[Category: Eg5]]
[[Category: Gtp-binding]]
[[Category: Homology model]]
[[Category: Kinesin]]
[[Category: Kinesin-5]]
[[Category: Klp61f]]
[[Category: Microtubule]]
[[Category: Mitosis]]
[[Category: Motor protein]]
[[Category: Nucleotide-binding]]
[[Category: Phosphoprotein]]
[[Category: Structural protein]]
[[Category: Tubulin]]