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==C-terminal motor and motor homology domain of Kar3Vik1 fused to a synthetic heterodimeric coiled coil== | |||
<StructureSection load='4etp' size='340' side='right' caption='[[4etp]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4etp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ETP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ETP FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=EBC:N,N-ETHANE-1,2-DIYLBIS(2-IODOACETAMIDE)'>EBC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3kar|3kar]], [[2o0a|2o0a]], [[1n6m|1n6m]], [[1u0i|1u0i]], [[1f9t|1f9t]], [[1f9u|1f9u]], [[1f9v|1f9v]], [[1f9w|1f9w]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KAR3, kar3p, P9659.16, YPR141C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Saccharomyces cerevisiae S288c]), VIK1, Vik1p, YPL253C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Saccharomyces cerevisiae S288c])</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=4etp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4etp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4etp RCSB], [http://www.ebi.ac.uk/pdbsum/4etp PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Kinesin-14 motors generate microtubule minus-end-directed force used in mitosis and meiosis. These motors are dimeric and operate with a nonprocessive powerstroke mechanism, but the role of the second head in motility has been unclear. In Saccharomyces cerevisiae, the Kinesin-14 Kar3 forms a heterodimer with either Vik1 or Cik1. Vik1 contains a motor homology domain that retains microtubule binding properties but lacks a nucleotide binding site. In this case, both heads are implicated in motility. Here, we show through structural determination of a C-terminal heterodimeric Kar3Vik1, electron microscopy, equilibrium binding, and motility that at the start of the cycle, Kar3Vik1 binds to or occludes two alphabeta-tubulin subunits on adjacent protofilaments. The cycle begins as Vik1 collides with the microtubule followed by Kar3 microtubule association and ADP release, thereby destabilizing the Vik1-microtubule interaction and positioning the motor for the start of the powerstroke. The results indicate that head-head communication is mediated through the adjoining coiled coil. | |||
Kar3Vik1, a member of the kinesin-14 superfamily, shows a novel kinesin microtubule binding pattern.,Rank KC, Chen CJ, Cope J, Porche K, Hoenger A, Gilbert SP, Rayment I J Cell Biol. 2012 Jun 25;197(7):957-70. doi: 10.1083/jcb.201201132. PMID:22734002<ref>PMID:22734002</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Saccharomyces cerevisiae s288c]] | [[Category: Saccharomyces cerevisiae s288c]] | ||
[[Category: Chen, C J | [[Category: Chen, C J]] | ||
[[Category: Cope, J | [[Category: Cope, J]] | ||
[[Category: Gilbert, S P | [[Category: Gilbert, S P]] | ||
[[Category: Hoenger, A | [[Category: Hoenger, A]] | ||
[[Category: Porche, K | [[Category: Porche, K]] | ||
[[Category: Rank, K C | [[Category: Rank, K C]] | ||
[[Category: Rayment, I | [[Category: Rayment, I]] | ||
[[Category: Internal vik1 crosslink with n]] | [[Category: Internal vik1 crosslink with n]] | ||
[[Category: Karyogamy]] | [[Category: Karyogamy]] | ||
Revision as of 13:52, 21 December 2014
C-terminal motor and motor homology domain of Kar3Vik1 fused to a synthetic heterodimeric coiled coilC-terminal motor and motor homology domain of Kar3Vik1 fused to a synthetic heterodimeric coiled coil
Structural highlights
Publication Abstract from PubMedKinesin-14 motors generate microtubule minus-end-directed force used in mitosis and meiosis. These motors are dimeric and operate with a nonprocessive powerstroke mechanism, but the role of the second head in motility has been unclear. In Saccharomyces cerevisiae, the Kinesin-14 Kar3 forms a heterodimer with either Vik1 or Cik1. Vik1 contains a motor homology domain that retains microtubule binding properties but lacks a nucleotide binding site. In this case, both heads are implicated in motility. Here, we show through structural determination of a C-terminal heterodimeric Kar3Vik1, electron microscopy, equilibrium binding, and motility that at the start of the cycle, Kar3Vik1 binds to or occludes two alphabeta-tubulin subunits on adjacent protofilaments. The cycle begins as Vik1 collides with the microtubule followed by Kar3 microtubule association and ADP release, thereby destabilizing the Vik1-microtubule interaction and positioning the motor for the start of the powerstroke. The results indicate that head-head communication is mediated through the adjoining coiled coil. Kar3Vik1, a member of the kinesin-14 superfamily, shows a novel kinesin microtubule binding pattern.,Rank KC, Chen CJ, Cope J, Porche K, Hoenger A, Gilbert SP, Rayment I J Cell Biol. 2012 Jun 25;197(7):957-70. doi: 10.1083/jcb.201201132. PMID:22734002[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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