5djn
From Proteopedia
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| - | ''' | + | ==Crystal structure of the Kinesin-3 KIF13A NC-CC1 mutant - Deletion of P390== |
| + | <StructureSection load='5djn' size='340' side='right' caption='[[5djn]], [[Resolution|resolution]] 2.82Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5djn]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DJN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DJN FirstGlance]. <br> | ||
| + | </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=5djn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5djn OCA], [http://pdbe.org/5djn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5djn RCSB], [http://www.ebi.ac.uk/pdbsum/5djn 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 5djn" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | + | <references/> | |
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Feng, W]] | [[Category: Feng, W]] | ||
| + | [[Category: Ren, J Q]] | ||
| + | [[Category: Coil-coil]] | ||
| + | [[Category: Transport protein]] | ||
Revision as of 19:32, 30 December 2015
Crystal structure of the Kinesin-3 KIF13A NC-CC1 mutant - Deletion of P390
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