3lre

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:42, 6 September 2023) (edit) (undo)
 
(5 intermediate revisions not shown.)
Line 1: Line 1:
-
{{STRUCTURE_3lre| PDB=3lre | SCENE= }}
 
-
===Crystal Structure Analysis of Human Kinesin-8 Motor Domain===
 
-
{{ABSTRACT_PUBMED_20818331}}
 
-
==Function==
+
==Crystal Structure Analysis of Human Kinesin-8 Motor Domain==
-
[[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>
+
<StructureSection load='3lre' size='340' side='right'caption='[[3lre]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 +
== Structural highlights ==
 +
<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>
 +
</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>
 +
<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>
 +
<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>
 +
</table>
 +
== Function ==
 +
[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>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
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.
-
==About this Structure==
+
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>
-
[[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].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<ref group="xtra">PMID:020818331</ref><references group="xtra"/><references/>
+
</div>
 +
<div class="pdbe-citations 3lre" style="background-color:#fffaf0;"></div>
 +
 
 +
==See Also==
 +
*[[Kinesin 3D Structures|Kinesin 3D Structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Brejc, K.]]
+
[[Category: Large Structures]]
-
[[Category: Hartman, J.]]
+
[[Category: Brejc K]]
-
[[Category: Moores, C A.]]
+
[[Category: Hartman J]]
-
[[Category: Atp-binding]]
+
[[Category: Moores CA]]
-
[[Category: Cell projection]]
+
-
[[Category: Cytoskeleton]]
+
-
[[Category: Glycoprotein]]
+
-
[[Category: Microtubule]]
+
-
[[Category: Microtubule binding]]
+
-
[[Category: Motor protein]]
+
-
[[Category: Nucleotide binding]]
+
-
[[Category: Nucleotide-binding]]
+
-
[[Category: Nucleus]]
+
-
[[Category: Phosphoprotein]]
+
-
[[Category: Protein transport]]
+
-
[[Category: Transport]]
+

Current revision

Crystal Structure Analysis of Human Kinesin-8 Motor Domain

PDB ID 3lre

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3lre"
Personal tools