4hna: Difference between revisions
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==Kinesin motor domain in the ADP-MG-ALFX state in complex with tubulin and a DARPIN== | |||
<StructureSection load='4hna' size='340' side='right' caption='[[4hna]], [[Resolution|resolution]] 3.19Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4hna]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Alfaropsis_roxburghiana Alfaropsis roxburghiana], [http://en.wikipedia.org/wiki/Ovis_aries Ovis aries] and [http://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HNA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HNA 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=ALF:TETRAFLUOROALUMINATE+ION'>ALF</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></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KIF5B, KNS, KNS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=139932 Alfaropsis roxburghiana])</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=4hna FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hna OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hna RCSB], [http://www.ebi.ac.uk/pdbsum/4hna PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The typical function of kinesins is to transport cargo along microtubules. Binding of ATP to microtubule-attached motile kinesins leads to cargo displacement. To better understand the nature of the conformational changes that lead to the power stroke that moves a kinesin's load along a microtubule, we determined the X-ray structure of human kinesin-1 bound to alphabeta-tubulin. The structure defines the mechanism of microtubule-stimulated ATP hydrolysis, which releases the kinesin motor domain from microtubules. It also reveals the structural linkages that connect the ATP nucleotide to the kinesin neck linker, a 15-amino acid segment C terminal to the catalytic core of the motor domain, to result in the power stroke. ATP binding to the microtubule-bound kinesin favors neck-linker docking. This biases the attachment of kinesin's second head in the direction of the movement, thus initiating each of the steps taken. | |||
Structure of a kinesin-tubulin complex and implications for kinesin motility.,Gigant B, Wang W, Dreier B, Jiang Q, Pecqueur L, Pluckthun A, Wang C, Knossow M Nat Struct Mol Biol. 2013 Aug;20(8):1001-7. doi: 10.1038/nsmb.2624. Epub 2013 Jul, 21. PMID:23872990<ref>PMID:23872990</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Kinesin|Kinesin]] | |||
*[[Tubulin|Tubulin]] | *[[Tubulin|Tubulin]] | ||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Alfaropsis roxburghiana]] | [[Category: Alfaropsis roxburghiana]] | ||
[[Category: Ovis aries]] | [[Category: Ovis aries]] | ||
[[Category: Synthetic construct]] | [[Category: Synthetic construct]] | ||
[[Category: Gigant, B | [[Category: Gigant, B]] | ||
[[Category: Knossow, M | [[Category: Knossow, M]] | ||
[[Category: Alpha-tubulin]] | [[Category: Alpha-tubulin]] | ||
[[Category: Beta-tubulin]] | [[Category: Beta-tubulin]] | ||
Revision as of 12:25, 21 December 2014
Kinesin motor domain in the ADP-MG-ALFX state in complex with tubulin and a DARPIN
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