5djo: Difference between revisions
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''' | ==Crystal structure of the CC1-FHA tandem of Kinesin-3 KIF13A== | ||
<StructureSection load='5djo' size='340' side='right' caption='[[5djo]], [[Resolution|resolution]] 1.74Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5djo]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DJO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DJO FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5djn|5djn]]</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=5djo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5djo OCA], [http://pdbe.org/5djo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5djo RCSB], [http://www.ebi.ac.uk/pdbsum/5djo PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Processive kinesin motors often contain a coiled-coil neck that controls the directionality and processivity. However, the neck coil (NC) of kinesin-3 is too short to form a stable coiled-coil dimer. Here, we found that the CC1-FHA tandem (that is connected to NC by P390) of kinesin-3 KIF13A assembles as an extended dimer. With the removal of P390, the NC-CC1 tandem of KIF13A unexpectedly forms a continuous coiled-coil dimer that can be well aligned into the CC1-FHA dimer. The reverse introduction of P390 breaks the NC-CC1 coiled-coil dimer but provides the intrinsic flexibility to couple NC with the CC1-FHA tandem. Mutations of either NC, CC1 or the FHA domain all significantly impaired the motor activity. Thus, the three elements within the NC-CC1-FHA tandem of KIF13A are structurally interrelated to form a stable dimer for activating the motor. This work also provides the first direct structural evidence to support the formation of a coiled-coil neck by the short characteristic neck domain of kinesin-3. | |||
Structural correlation of the neck coil with the CC1-FHA tandem for active kinesin-3 KIF13A.,Ren J, Huo L, Wang W, Zhang Y, Li W, Lou J, Xu T, Feng W J Biol Chem. 2015 Dec 17. pii: jbc.M115.689091. PMID:26680000<ref>PMID:26680000</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5djo" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Feng, W]] | [[Category: Feng, W]] | ||
[[Category: Huo, L]] | [[Category: Huo, L]] | ||
[[Category: Li, W]] | |||
[[Category: Ren, J Q]] | |||
[[Category: Coiled-coil]] | |||
[[Category: Fha domain]] | |||
[[Category: Transport protein]] | |||
Revision as of 19:31, 30 December 2015
Crystal structure of the CC1-FHA tandem of Kinesin-3 KIF13A
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