5djn: Difference between revisions

Line 1:

'''~~Unreleased~~ structure'''

==Crystal structure of the Kinesin-3 KIF13A NC-CC1 mutant - Deletion of P390==

== 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>

== 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.

~~The entry 5djn is ON HOLD until Paper Publication~~

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>

~~Authors: Ren~~, J.Q.~~, Feng, W~~.

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

~~Description: Crystal structure of the Kinesin~~-~~3 KIF13A NC~~-~~CC1 mutant -Deletion of P390~~

~~[[Category: Unreleased Structures]]~~

== References ==

~~[[Category: Ren, J.Q]]~~

__TOC__

</StructureSection>

[[Category: Feng, W]]

[[Category: Ren, J Q]]

[[Category: Coil-coil]]

[[Category: Transport protein]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==Crystal structure of the Kinesin-3 KIF13A NC-CC1 mutant - Deletion of P390==
+<StructureSection load='5djn' size='340' side='right' caption='[[5djn]], [[Resolution|resolution]] 2.82&Aring;' 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.
-The entry 5djn is ON HOLD  until Paper Publication
+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>
-Authors: Ren, J.Q., Feng, W.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: Crystal structure of the Kinesin-3 KIF13A NC-CC1 mutant -Deletion of P390
+<div class="pdbe-citations 5djn" style="background-color:#fffaf0;"></div>
-[[Category: Unreleased Structures]]
+== References ==
-[[Category: Ren, J.Q]]
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Feng, W]]
+[[Category: Ren, J Q]]
+[[Category: Coil-coil]]
+[[Category: Transport protein]]