View source for 5xxv


==GDP-microtubule complexed with KIF5C in AMPPNP state==
<SX load='5xxv' size='340' side='right' viewer='molstar' caption='[[5xxv]], [[Resolution|resolution]] 6.46&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5xxv]] is a 18 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XXV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XXV FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 6.46&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5xxv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xxv OCA], [https://pdbe.org/5xxv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xxv RCSB], [https://www.ebi.ac.uk/pdbsum/5xxv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xxv ProSAT]</span></td></tr>
</table>
== Function ==
[https://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.
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== Publication Abstract from PubMed ==
Kinesin-1, the founding member of the kinesin superfamily of proteins, is known to use only a subset of microtubules for transport in living cells. This biased use of microtubules is proposed as the guidance cue for polarized transport in neurons, but the underlying mechanisms are still poorly understood. Here, we report that kinesin-1 binding changes the microtubule lattice and promotes further kinesin-1 binding. This high-affinity state requires the binding of kinesin-1 in the nucleotide-free state. Microtubules return to the initial low-affinity state by washing out the binding kinesin-1 or by the binding of non-hydrolyzable ATP analogue AMPPNP to kinesin-1. X-ray fiber diffraction, fluorescence speckle microscopy, and second-harmonic generation microscopy, as well as cryo-EM, collectively demonstrated that the binding of nucleotide-free kinesin-1 to GDP microtubules changes the conformation of the GDP microtubule to a conformation resembling the GTP microtubule.

Kinesin-binding-triggered conformation switching of microtubules contributes to polarized transport.,Shima T, Morikawa M, Kaneshiro J, Kambara T, Kamimura S, Yagi T, Iwamoto H, Uemura S, Shigematsu H, Shirouzu M, Ichimura T, Watanabe TM, Nitta R, Okada Y, Hirokawa N J Cell Biol. 2018 Oct 8. pii: jcb.201711178. doi: 10.1083/jcb.201711178. PMID:30297389<ref>PMID:30297389</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5xxv" style="background-color:#fffaf0;"></div>

==See Also==
*[[Tubulin 3D Structures|Tubulin 3D Structures]]
== References ==
<references/>
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[[Category: Large Structures]]
[[Category: Sus scrofa]]
[[Category: Hirokawa N]]
[[Category: Morikawa M]]
[[Category: Nitta R]]
[[Category: Shigematsu H]]