3wrd: Difference between revisions
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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=''> | ||
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<table><tr><td colspan='2'>[[3wrd]] is a 2 chain structure. 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. 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> | ||
</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"><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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wrd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wrd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wrd RCSB], [http://www.ebi.ac.uk/pdbsum/3wrd PDBsum]</span></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> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3wrd" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 16:30, 4 May 2017
Crystal Structure of the KIF5C Motor Domain Without Any NucleotideCrystal Structure of the KIF5C Motor Domain Without Any Nucleotide
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 PubMedThe 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. References
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