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5hnw
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structural basis of backwards motion in kinesin-14: minus-end directed nKn664 in the AMPPNP state== | |
| + | <SX load='5hnw' size='340' side='right' viewer='molstar' caption='[[5hnw]], [[Resolution|resolution]] 6.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5hnw]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus], [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HNW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HNW 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]] 6.6Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <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>, <scene name='pdbligand=TA1:TAXOL'>TA1</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=5hnw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hnw OCA], [https://pdbe.org/5hnw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hnw RCSB], [https://www.ebi.ac.uk/pdbsum/5hnw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hnw ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/NCD_DROME NCD_DROME] NCD is required for normal chromosomal segregation in meiosis, in females, and in early mitotic divisions of the embryo. The NCD motor activity is directed toward the microtubule's minus end.<ref>PMID:2146510</ref> [https://www.uniprot.org/uniprot/KIF5C_RAT KIF5C_RAT] Microtubule-associated force-producing protein that may play a role in organelle transport (By similarity). Has ATPase activity (PubMed:27452403). Involved in synaptic transmission (By similarity). Mediates dendritic trafficking of mRNAs (By similarity). Required for anterograde axonal transportation of MAPK8IP3/JIP3 which is essential for MAPK8IP3/JIP3 function in axon elongation (PubMed:23576431).[UniProtKB:O60282][UniProtKB:P28738]<ref>PMID:23576431</ref> <ref>PMID:27452403</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Kinesin-14 is a unique minus-end-directed microtubule-based motor. A swinging motion of a class-specific N-terminal neck helix has been proposed to produce minus-end directionality. However, it is unclear how swinging of the neck helix is driven by ATP hydrolysis utilizing the highly conserved catalytic core among all kinesins. Here, using a motility assay, we show that in addition to the neck helix, the conserved five residues at the C-terminal region in kinesin-14, namely the neck mimic, are necessary to give kinesin-1 an ability to reverse its directionality toward the minus end of microtubules. Our structural analyses further demonstrate that the C-terminal neck mimic, in cooperation with conformational changes in the catalytic core during ATP binding, forms a kinesin-14 bundle with the N-terminal neck helix to swing toward the minus end of microtubules. Thus, the neck mimic plays a crucial role in coupling the chemical ATPase reaction with the mechanical cycle to produce the minus-end-directed motility of kinesin-14. | ||
| - | + | Structural Basis of Backwards Motion in Kinesin-1-Kinesin-14 Chimera: Implication for Kinesin-14 Motility.,Yamagishi M, Shigematsu H, Yokoyama T, Kikkawa M, Sugawa M, Aoki M, Shirouzu M, Yajima J, Nitta R Structure. 2016 Aug 2;24(8):1322-34. doi: 10.1016/j.str.2016.05.021. Epub 2016, Jul 21. PMID:27452403<ref>PMID:27452403</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5hnw" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | |
| - | [[Category: Shigematsu | + | ==See Also== |
| - | [[Category: Shirouzu | + | *[[Tubulin 3D Structures|Tubulin 3D Structures]] |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </SX> | ||
| + | [[Category: Bos taurus]] | ||
| + | [[Category: Drosophila melanogaster]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Rattus norvegicus]] | ||
| + | [[Category: Kikkawa M]] | ||
| + | [[Category: Nitta R]] | ||
| + | [[Category: Shigematsu H]] | ||
| + | [[Category: Shirouzu M]] | ||
| + | [[Category: Yokoyama T]] | ||
Current revision
Structural basis of backwards motion in kinesin-14: minus-end directed nKn664 in the AMPPNP state
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