3lre

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{{STRUCTURE_3lre| PDB=3lre | SCENE= }}
 
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===Crystal Structure Analysis of Human Kinesin-8 Motor Domain===
 
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{{ABSTRACT_PUBMED_20818331}}
 
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==Function==
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==Crystal Structure Analysis of Human Kinesin-8 Motor Domain==
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[[http://www.uniprot.org/uniprot/KI18A_HUMAN KI18A_HUMAN]] Microtubule-depolymerizing kinesin which plays a role in chromosome congression by reducing the amplitude of preanaphase oscillations and slowing poleward movement during anaphase, thus suppressing chromosome movements. May stabilize the CENPE-BUB1B complex at the kinetochores during early mitosis and maintains CENPE levels at kinetochores during chromosome congression.<ref>PMID:17346968</ref> <ref>PMID:18267093</ref> <ref>PMID:18513970</ref> <ref>PMID:19625775</ref>
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<StructureSection load='3lre' size='340' side='right'caption='[[3lre]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3lre]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LRE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LRE FirstGlance]. <br>
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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]] 2.2&#8491;</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=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3lre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lre OCA], [https://pdbe.org/3lre PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lre RCSB], [https://www.ebi.ac.uk/pdbsum/3lre PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lre ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/KI18A_HUMAN KI18A_HUMAN] Microtubule-depolymerizing kinesin which plays a role in chromosome congression by reducing the amplitude of preanaphase oscillations and slowing poleward movement during anaphase, thus suppressing chromosome movements. May stabilize the CENPE-BUB1B complex at the kinetochores during early mitosis and maintains CENPE levels at kinetochores during chromosome congression.<ref>PMID:17346968</ref> <ref>PMID:18267093</ref> <ref>PMID:18513970</ref> <ref>PMID:19625775</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Members of the kinesin-8 motor class have the remarkable ability to both walk towards microtubule plus-ends and depolymerise these ends on arrival, thereby regulating microtubule length. To analyse how kinesin-8 multitasks, we studied the structure and function of the kinesin-8 motor domain. We determined the first crystal structure of a kinesin-8 and used cryo-electron microscopy to calculate the structure of the microtubule-bound motor. Microtubule-bound kinesin-8 reveals a new conformation compared with the crystal structure, including a bent conformation of the alpha4 relay helix and ordering of functionally important loops. The kinesin-8 motor domain does not depolymerise stabilised microtubules with ATP but does form tubulin rings in the presence of a non-hydrolysable ATP analogue. This shows that, by collaborating, kinesin-8 motor domain molecules can release tubulin from microtubules, and that they have a similar mechanical effect on microtubule ends as kinesin-13, which enables depolymerisation. Our data reveal aspects of the molecular mechanism of kinesin-8 motors that contribute to their unique dual motile and depolymerising functions, which are adapted to control microtubule length.
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==About this Structure==
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Insight into the molecular mechanism of the multitasking kinesin-8 motor.,Peters C, Brejc K, Belmont L, Bodey AJ, Lee Y, Yu M, Guo J, Sakowicz R, Hartman J, Moores CA EMBO J. 2010 Oct 20;29(20):3437-47. Epub 2010 Sep 3. PMID:20818331<ref>PMID:20818331</ref>
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[[3lre]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LRE OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<ref group="xtra">PMID:020818331</ref><references group="xtra"/><references/>
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</div>
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<div class="pdbe-citations 3lre" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Kinesin 3D Structures|Kinesin 3D Structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Brejc, K.]]
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[[Category: Large Structures]]
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[[Category: Hartman, J.]]
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[[Category: Brejc K]]
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[[Category: Moores, C A.]]
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[[Category: Hartman J]]
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[[Category: Atp-binding]]
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[[Category: Moores CA]]
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[[Category: Cell projection]]
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[[Category: Cytoskeleton]]
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[[Category: Glycoprotein]]
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[[Category: Microtubule]]
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[[Category: Microtubule binding]]
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[[Category: Motor protein]]
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[[Category: Nucleotide binding]]
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[[Category: Nucleotide-binding]]
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[[Category: Nucleus]]
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[[Category: Phosphoprotein]]
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[[Category: Protein transport]]
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[[Category: Transport]]
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Current revision

Crystal Structure Analysis of Human Kinesin-8 Motor Domain

PDB ID 3lre

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