3u06

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Current revision (10:16, 1 March 2024) (edit) (undo)
 
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<StructureSection load='3u06' size='340' side='right'caption='[[3u06]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
<StructureSection load='3u06' size='340' side='right'caption='[[3u06]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3u06]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U06 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U06 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3u06]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U06 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U06 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CA(ND), CG7831, ncd, non-claret disjunctional ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=3u06 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u06 OCA], [https://pdbe.org/3u06 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u06 RCSB], [https://www.ebi.ac.uk/pdbsum/3u06 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u06 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=3u06 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u06 OCA], [https://pdbe.org/3u06 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u06 RCSB], [https://www.ebi.ac.uk/pdbsum/3u06 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u06 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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>
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Rotation of the coiled-coil stalk of the kinesin-14 motors is thought to drive displacements or steps by the motor along microtubules, but the structural changes that trigger stalk rotation and the nucleotide state in which it occurs are not certain. Here we report a kinesin-14 neck mutant that releases ADP more slowly than wild type and shows weaker microtubule affinity, consistent with defective stalk rotation. Unexpectedly, crystal structures show the stalk fully rotated - neck-motor interactions destabilize the stalk, causing it to rotate and ADP to be released, and alter motor affinity for microtubules. A new structural pathway accounts for the coupling of stalk rotation - the force-producing stroke - to changes in motor affinity for nucleotide and microtubules. Sequential disruption of salt bridges that stabilize the unrotated stalk could cause the stalk to initiate and complete rotation in different nucleotide states.
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Neck-motor interactions trigger rotation of the kinesin stalk.,Liu HL, Pemble Iv CW, Endow SA Sci Rep. 2012;2:236. Epub 2012 Jan 27. PMID:22355749<ref>PMID:22355749</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3u06" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Drome]]
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[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Endow, S A]]
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[[Category: Endow SA]]
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[[Category: IV, C W.Pemble]]
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[[Category: Liu H-L]]
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[[Category: Liu, H L]]
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[[Category: Pemble IV CW]]
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[[Category: Atp binding]]
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[[Category: Cell division]]
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[[Category: Kinesin-14]]
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[[Category: Microtubule]]
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[[Category: Microtubule binding]]
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[[Category: Molecular motor]]
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[[Category: Motor domain]]
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[[Category: Motor protein]]
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[[Category: Ncd]]
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[[Category: Power stroke]]
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[[Category: Stalk rotation]]
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[[Category: Transport]]
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Current revision

Crystal structure of the kinesin-14 NcdG347D

PDB ID 3u06

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Proteopedia Page Contributors and Editors (what is this?)

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