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5hnw

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Structural basis of backwards motion in kinesin-14: minus-end directed nKn664 in the AMPPNP state

5hnw, resolution 6.60Å

Structural highlights

5hnw is a 3 chain structure with sequence from Bos taurus, Drosophila melanogaster and Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 6.6Å
Ligands:
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1] 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]^[2] ^[3]

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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Walker RA, Salmon ED, Endow SA. The Drosophila claret segregation protein is a minus-end directed motor molecule. Nature. 1990 Oct 25;347(6295):780-2. PMID:2146510 doi:http://dx.doi.org/10.1038/347780a0
↑ Sun T, Yu N, Zhai LK, Li N, Zhang C, Zhou L, Huang Z, Jiang XY, Shen Y, Chen ZY. c-Jun NH2-terminal kinase (JNK)-interacting protein-3 (JIP3) regulates neuronal J Biol Chem. 2013 May 17;288(20):14531-14543. PMID:23576431 doi:10.1074/jbc.M113.464453
↑ Yamagishi M, Shigematsu H, Yokoyama T, Kikkawa M, Sugawa M, Aoki M, Shirouzu M, Yajima J, Nitta R. Structural Basis of Backwards Motion in Kinesin-1-Kinesin-14 Chimera: Implication for Kinesin-14 Motility. Structure. 2016 Aug 2;24(8):1322-34. doi: 10.1016/j.str.2016.05.021. Epub 2016, Jul 21. PMID:27452403 doi:http://dx.doi.org/10.1016/j.str.2016.05.021
↑ Yamagishi M, Shigematsu H, Yokoyama T, Kikkawa M, Sugawa M, Aoki M, Shirouzu M, Yajima J, Nitta R. Structural Basis of Backwards Motion in Kinesin-1-Kinesin-14 Chimera: Implication for Kinesin-14 Motility. Structure. 2016 Aug 2;24(8):1322-34. doi: 10.1016/j.str.2016.05.021. Epub 2016, Jul 21. PMID:27452403 doi:http://dx.doi.org/10.1016/j.str.2016.05.021

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5hnw"

@@ Line 1: / Line 1: @@
 ==Structural basis of backwards motion in kinesin-14: minus-end directed nKn664 in the AMPPNP state==
-<StructureSection load='5hnw' size='340' side='right' caption='[[5hnw]], [[Resolution|resolution]] 6.60&Aring;' scene=''>
+<SX load='5hnw' size='340' side='right' viewer='molstar' caption='[[5hnw]], [[Resolution|resolution]] 6.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5hnw]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Drome Drome]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HNW FirstGlance]. <br>
+<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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 6.6&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ncd, CA(ND), CG7831 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5hnw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hnw OCA], [http://pdbe.org/5hnw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hnw RCSB], [http://www.ebi.ac.uk/pdbsum/5hnw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hnw 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=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 ==
-[[http://www.uniprot.org/uniprot/TBA1B_BOVIN TBA1B_BOVIN]] 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/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>  [[http://www.uniprot.org/uniprot/TBB2B_BOVIN TBB2B_BOVIN]] 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 (By similarity).
+[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 ==
@@ Line 19: / Line 19: @@
 </div>
 <div class="pdbe-citations 5hnw" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Tubulin 3D Structures|Tubulin 3D Structures]]
 == References ==
 <references/>
 __TOC__
-</StructureSection>
+</SX>
 [[Category: Bos taurus]]
-[[Category: Drome]]
+[[Category: Drosophila melanogaster]]
-[[Category: Kikkawa, M]]
+[[Category: Large Structures]]
-[[Category: Nitta, R]]
+[[Category: Rattus norvegicus]]
-[[Category: Shigematsu, H]]
+[[Category: Kikkawa M]]
-[[Category: Shirouzu, M]]
+[[Category: Nitta R]]
-[[Category: Yokoyama, T]]
+[[Category: Shigematsu H]]
-[[Category: Atpase]]
+[[Category: Shirouzu M]]
-[[Category: Kinesin]]
+[[Category: Yokoyama T]]
-[[Category: Kinesin-14]]
-[[Category: Microtubule]]
-[[Category: Transport protein]]

5hnw

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Current revision

Structural basis of backwards motion in kinesin-14: minus-end directed nKn664 in the AMPPNP state

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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