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| | ==Crystal Structure of the KIF5C Motor Domain Without Any Nucleotide== | | ==Crystal Structure of the KIF5C Motor Domain Without Any Nucleotide== |
| - | <StructureSection load='3wrd' size='340' side='right' caption='[[3wrd]], [[Resolution|resolution]] 2.86Å' scene=''> | + | <StructureSection load='3wrd' size='340' side='right'caption='[[3wrd]], [[Resolution|resolution]] 2.86Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3wrd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WRD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WRD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3wrd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WRD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WRD FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Kif5c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Kif5c ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=3wrd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wrd OCA], [http://pdbe.org/3wrd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wrd RCSB], [http://www.ebi.ac.uk/pdbsum/3wrd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wrd ProSAT]</span></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=3wrd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wrd OCA], [https://pdbe.org/3wrd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wrd RCSB], [https://www.ebi.ac.uk/pdbsum/3wrd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wrd ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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> | + | [[https://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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Kinesin|Kinesin]] | + | *[[Kinesin 3D Structures|Kinesin 3D Structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Lk3 transgenic mice]] | | [[Category: Lk3 transgenic mice]] |
| | [[Category: Hirokawa, N]] | | [[Category: Hirokawa, N]] |
| Structural highlights
Function
[KIF5C_MOUSE] Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. Mediates dendritic trafficking of mRNAs.[1]
Publication Abstract from PubMed
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.
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kindler S, Dieterich DC, Schutt J, Sahin J, Karpova A, Mikhaylova M, Schob C, Gundelfinger ED, Kreienkamp HJ, Kreutz MR. Dendritic mRNA targeting of Jacob and N-methyl-d-aspartate-induced nuclear translocation after calpain-mediated proteolysis. J Biol Chem. 2009 Sep 11;284(37):25431-40. doi: 10.1074/jbc.M109.022137. Epub, 2009 Jul 16. PMID:19608740 doi:http://dx.doi.org/10.1074/jbc.M109.022137
- ↑ Morikawa M, Yajima H, Nitta R, Inoue S, Ogura T, Sato C, Hirokawa N. X-ray and Cryo-EM structures reveal mutual conformational changes of Kinesin and GTP-state microtubules upon binding. EMBO J. 2015 Mar 16. pii: e201490588. PMID:25777528 doi:http://dx.doi.org/10.15252/embj.201490588
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