5djo

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==Crystal structure of the CC1-FHA tandem of Kinesin-3 KIF13A==
==Crystal structure of the CC1-FHA tandem of Kinesin-3 KIF13A==
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<StructureSection load='5djo' size='340' side='right' caption='[[5djo]], [[Resolution|resolution]] 1.74&Aring;' scene=''>
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<StructureSection load='5djo' size='340' side='right'caption='[[5djo]], [[Resolution|resolution]] 1.74&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<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>
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<table><tr><td colspan='2'>[[5djo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5DJO FirstGlance]. <br>
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</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>
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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]] 1.74&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5djn|5djn]]</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=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
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<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>
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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=5djo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5djo OCA], [https://pdbe.org/5djo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5djo RCSB], [https://www.ebi.ac.uk/pdbsum/5djo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5djo ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/KI13A_MOUSE KI13A_MOUSE] Plus end-directed microtubule-dependent motor protein involved in intracellular transport and regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane, endosomal sorting during melanosome biogenesis and cytokinesis. During melanosome maturation, required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. Also required for the abcission step in cytokinesis: mediates translocation of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis (By similarity). Mediates the transport of M6PR-containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex.<ref>PMID:11106728</ref>
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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.
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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>
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==See Also==
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*[[Kinesin 3D Structures|Kinesin 3D Structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5djo" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Feng, W]]
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[[Category: Large Structures]]
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[[Category: Huo, L]]
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[[Category: Mus musculus]]
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[[Category: Li, W]]
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[[Category: Feng W]]
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[[Category: Ren, J Q]]
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[[Category: Huo L]]
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[[Category: Coiled-coil]]
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[[Category: Li W]]
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[[Category: Fha domain]]
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[[Category: Ren JQ]]
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[[Category: Transport protein]]
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Current revision

Crystal structure of the CC1-FHA tandem of Kinesin-3 KIF13A

PDB ID 5djo

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