View source for 5lt4


==nucleotide-free kinesin-1 motor domain T92V mutant, P1 crystal form==
<StructureSection load='5lt4' size='340' side='right'caption='[[5lt4]], [[Resolution|resolution]] 2.88&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5lt4]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LT4 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5LT4 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5lt4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lt4 OCA], [http://pdbe.org/5lt4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lt4 RCSB], [http://www.ebi.ac.uk/pdbsum/5lt4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lt4 ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/KINH_HUMAN KINH_HUMAN]] Microtubule-dependent motor required for normal distribution of mitochondria and lysosomes (By similarity). 
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5lt4" style="background-color:#fffaf0;"></div>

==See Also==
*[[Kinesin 3D Structures|Kinesin 3D Structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Cao, L]]
[[Category: Gigant, B]]
[[Category: Adp dissociation]]
[[Category: Kinesin motor domain]]
[[Category: Motor protein]]
[[Category: Nucleotide-free]]