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5lt1
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==nucleotide-free kinesin-1 motor domain T92V mutant, P21 crystal form== | |
| + | <StructureSection load='5lt1' size='340' side='right' caption='[[5lt1]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5lt1]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LT1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LT1 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=SR:STRONTIUM+ION'>SR</scene></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=5lt1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lt1 OCA], [http://pdbe.org/5lt1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lt1 RCSB], [http://www.ebi.ac.uk/pdbsum/5lt1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lt1 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Kinesin-1 is an ATP-dependent motor protein that moves towards microtubules (+)-ends. Whereas structures of isolated ADP-kinesin and of complexes with tubulin of apo-kinesin and of ATP-like-kinesin are available, structural data on apo-kinesin-1 in the absence of tubulin are still missing, leaving the role of nucleotide release in the structural cycle unsettled. Here, we identified mutations in the kinesin nucleotide-binding P-loop motif that interfere with ADP binding. These mutations destabilize the P-loop (T87A mutant) or magnesium binding (T92V), highlighting a dual mechanism for nucleotide release. The structures of these mutants in their apo form are either isomorphous to ADP-kinesin-1 or to tubulin-bound apo-kinesin-1. Remarkably, both structures are also obtained from the nucleotide-depleted wild-type protein. Our results lead to a model in which, when detached from microtubules, apo-kinesin possibly occupies the two conformations we characterized, whereas, upon microtubule binding, ADP-kinesin converts to the tubulin-bound apo-kinesin conformation and releases ADP. This conformation is primed to bind ATP and, therefore, to run through the natural nucleotide cycle of kinesin-1. | ||
| - | + | The structural switch of nucleotide-free kinesin.,Cao L, Cantos-Fernandes S, Gigant B Sci Rep. 2017 Feb 14;7:42558. doi: 10.1038/srep42558. PMID:28195215<ref>PMID:28195215</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5lt1" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Cao, L]] | ||
| + | [[Category: Gigant, B]] | ||
| + | [[Category: Adp dissociation]] | ||
| + | [[Category: Kinesin motor domain]] | ||
| + | [[Category: Motor protein]] | ||
| + | [[Category: Nucleotide-free]] | ||
Revision as of 09:37, 11 March 2017
nucleotide-free kinesin-1 motor domain T92V mutant, P21 crystal form
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