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| <StructureSection load='5x3e' size='340' side='right'caption='[[5x3e]], [[Resolution|resolution]] 2.61Å' scene=''> | | <StructureSection load='5x3e' size='340' side='right'caption='[[5x3e]], [[Resolution|resolution]] 2.61Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[5x3e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Caeel Caeel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X3E OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5X3E FirstGlance]. <br> | | <table><tr><td colspan='2'>[[5x3e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X3E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5X3E FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</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">X-ray diffraction, [[Resolution|Resolution]] 2.61Å</td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">zen-4, CELE_M03D4.1, M03D4.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</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'>[http://proteopedia.org/fgij/fg.htm?mol=5x3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x3e OCA], [http://pdbe.org/5x3e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x3e RCSB], [http://www.ebi.ac.uk/pdbsum/5x3e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x3e 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=5x3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x3e OCA], [https://pdbe.org/5x3e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5x3e RCSB], [https://www.ebi.ac.uk/pdbsum/5x3e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5x3e ProSAT]</span></td></tr> |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
| | == Function == |
| == Publication Abstract from PubMed == | | [https://www.uniprot.org/uniprot/G5EG83_CAEEL G5EG83_CAEEL] |
| Kinesins hydrolyse ATP to transport intracellular cargoes along microtubules. Kinesin neck linker (NL) functions as the central mechano-chemical coupling element by changing its conformation through the ATPase cycle. Here we report the crystal structure of kinesin-6 Zen4 in a nucleotide-free, apo state, with the NL initial segment (NIS) adopting a backward-docked conformation and the preceding alpha6 helix partially melted. Single-molecule fluorescence resonance energy transfer (smFRET) analyses indicate the NIS of kinesin-1 undergoes similar conformational changes under tension in the two-head bound (2HB) state, whereas it is largely disordered without tension. The backward-docked structure of NIS is essential for motility of the motor. Our findings reveal a key missing conformation of kinesins, which provides the structural basis of the stable 2HB state and offers a tension-based rationale for an optimal NL length to ensure processivity of the motor.
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| Crystal structure of Zen4 in the apo state reveals a missing conformation of kinesin.,Guan R, Zhang L, Su QP, Mickolajczyk KJ, Chen GY, Hancock WO, Sun Y, Zhao Y, Chen Z Nat Commun. 2017 Apr 10;8:14951. doi: 10.1038/ncomms14951. PMID:28393873<ref>PMID:28393873</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 5x3e" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[Kinesin 3D Structures|Kinesin 3D Structures]] | | *[[Kinesin 3D Structures|Kinesin 3D Structures]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Caeel]] | | [[Category: Caenorhabditis elegans]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Chen, Z]] | | [[Category: Chen Z]] |
| [[Category: Guan, R]] | | [[Category: Guan R]] |
| [[Category: Zhang, L]] | | [[Category: Zhang L]] |
| [[Category: Apo state]]
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| [[Category: Kinesin 6]]
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| [[Category: Motor protein]]
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| [[Category: Neck linker]]
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