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| ==Nucleotide-free Kinesin motor domain complexed with GMPCPP-microtubule== | | ==Nucleotide-free Kinesin motor domain complexed with GMPCPP-microtubule== |
| <StructureSection load='3j6h' size='340' side='right' caption='[[3j6h]], [[Resolution|resolution]] 8.10Å' scene=''> | | <SX load='3j6h' size='340' side='right' viewer='molstar' caption='[[3j6h]], [[Resolution|resolution]] 8.10Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[3j6h]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J6H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J6H FirstGlance]. <br> | | <table><tr><td colspan='2'>[[3j6h]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J6H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J6H FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=G2P:PHOSPHOMETHYLPHOSPHONIC+ACID+GUANYLATE+ESTER'>G2P</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 8.1Å</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=3j6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j6h OCA], [http://pdbe.org/3j6h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3j6h RCSB], [http://www.ebi.ac.uk/pdbsum/3j6h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3j6h ProSAT]</span></td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=G2P:PHOSPHOMETHYLPHOSPHONIC+ACID+GUANYLATE+ESTER'>G2P</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <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'>[https://proteopedia.org/fgij/fg.htm?mol=3j6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j6h OCA], [https://pdbe.org/3j6h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j6h RCSB], [https://www.ebi.ac.uk/pdbsum/3j6h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j6h ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://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. [[http://www.uniprot.org/uniprot/KIF5C_MOUSE KIF5C_MOUSE]] Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. Mediates dendritic trafficking of mRNAs.<ref>PMID:19608740</ref> [[http://www.uniprot.org/uniprot/TBB_PIG TBB_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. | | [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. |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| The molecular motor kinesin moves along microtubules using energy from ATP hydrolysis in an initial step coupled with ADP release. In neurons, kinesin-1/KIF5C preferentially binds to the GTP-state microtubules over GDP-state microtubules to selectively enter an axon among many processes; however, because the atomic structure of nucleotide-free KIF5C is unavailable, its molecular mechanism remains unresolved. Here, the crystal structure of nucleotide-free KIF5C and the cryo-electron microscopic structure of nucleotide-free KIF5C complexed with the GTP-state microtubule are presented. The structures illustrate mutual conformational changes induced by interaction between the GTP-state microtubule and KIF5C. KIF5C acquires the 'rigor conformation', where mobile switches I and II are stabilized through L11 and the initial portion of the neck-linker, facilitating effective ADP release and the weak-to-strong transition of KIF5C microtubule affinity. Conformational changes to tubulin strengthen the longitudinal contacts of the GTP-state microtubule in a similar manner to GDP-taxol microtubules. These results and functional analyses provide the molecular mechanism of the preferential binding of KIF5C to GTP-state microtubules.
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| X-ray and Cryo-EM structures reveal mutual conformational changes of Kinesin and GTP-state microtubules upon binding.,Morikawa M, Yajima H, Nitta R, Inoue S, Ogura T, Sato C, Hirokawa N EMBO J. 2015 Mar 16. pii: e201490588. PMID:25777528<ref>PMID:25777528</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 3j6h" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[Tubulin|Tubulin]] | | *[[Kinesin 3D Structures|Kinesin 3D Structures]] |
| == References ==
| | *[[Tubulin 3D Structures|Tubulin 3D Structures]] |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </SX> |
| | [[Category: Large Structures]] |
| | [[Category: Mus musculus]] |
| [[Category: Sus scrofa]] | | [[Category: Sus scrofa]] |
| [[Category: Hirokawa, N]] | | [[Category: Hirokawa N]] |
| [[Category: Inoue, S]] | | [[Category: Inoue S]] |
| [[Category: Morikawa, M]] | | [[Category: Morikawa M]] |
| [[Category: Nitta, R]] | | [[Category: Nitta R]] |
| [[Category: Ogura, T]] | | [[Category: Ogura T]] |
| [[Category: Sato, C]] | | [[Category: Sato C]] |
| [[Category: Yajima, H]] | | [[Category: Yajima H]] |
| [[Category: Axonal transport]]
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| [[Category: Gmpcpp-microtubule]]
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| [[Category: Kinesin]]
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| [[Category: Microtubule]]
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| [[Category: Motor domain]]
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| [[Category: Nucleotide-free kinesin]]
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| [[Category: Rigor-conformation]]
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| [[Category: Structural protein-motor protein complex]]
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| [[Category: Tubulin]]
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