Kinesin

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{{STRUCTURE_2zfi | PDB=2zfi | SIZE=350 | SCENE=Kinesin/Kinesin_start_scene/2 | CAPTION=KIF1A Motor Domain complex with ADP and Mg+2 ion (green), [[2zfi]] }}
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<StructureSection load='' size='350' side='right' scene='41/410296/Cv/1' caption='KIF1A Motor Domain complex with ADP and Mg+2 ion (green), [[2zfi]]'>
== Function ==
== Function ==
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[[Kinesin|Kinesins]] are eukaryotic motor proteins which move along microtubules<ref>PMID:19773780</ref>. Kinesin (KIF) is a dimer consisting of 2 heavy chains and two light chains. The heavy chain contains the N-terminal globular motor domain (MD) responsible for the motor activity of kinesin, a central flexible neck linker (FNL) coiled-coil stalk which intertwines to form the dimer and a small globular C-terminal domain which interacts with other proteins like the kinesin light chain. The light chain (KLC) forms the tail region. The KLC contains a cargo binding domain which is called TPR (Tetratricopeptide repeat). The KIFs are named by their gene number. KIF contains a forkhead-associated domain (FHA) which is involved in phosphopeptide recognition.<br />
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[[Kinesin|Kinesins]] are eukaryotic motor proteins which move along microtubules<ref>PMID:19773780</ref>. Kinesin (KIF) is a dimer consisting of 2 heavy chains and two light chains. The heavy chain contains the N-terminal globular motor domain (MD) residues 1-375, responsible for the motor activity of kinesin, a central flexible neck linker (FNL) coiled-coil stalk which intertwines to form the dimer and a small globular C-terminal domain which interacts with other proteins like the kinesin light chain. The light chain (KLC) forms the tail region. The KLC contains a cargo binding domain which is called TPR (Tetratricopeptide repeat). The KIFs are named by their gene number. KIF are organized into 14 families named kinesin-1 to kinesin-14. KIF contains a forkhead-associated domain (FHA) which is involved in phosphopeptide recognition.<br />
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*'''KIF1A''' transports organelles along axonal microtubules.<br />
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*'''KIF1C''' and '''KIF2''' are plus-ended directed microtubule motors.<br />
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*'''KIF2C''', '''KIF22''' and '''KIF3B''' are plus-ended directed microtubule motors in mitotic cells<br />
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*'''KIF13B''' transports VEGFR2 from the Golgi to the endothelial cell surface.<br />
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*'''KIF16B''' is plus-ended directed microtubule motor involved in endosome transport and receptor recycling.<br />
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*'''KIFC1''' transports DNA molecules along cytoskeleton filaments.<br />
*'''Kar3''' is kinesin protein in yeast.<br />
*'''Kar3''' is kinesin protein in yeast.<br />
*'''Eg5''' or '''KIF11''' is a kinesin (See [[Kinesin-5]]) which participates in mitosis.<br />
*'''Eg5''' or '''KIF11''' is a kinesin (See [[Kinesin-5]]) which participates in mitosis.<br />
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== Disease ==
== Disease ==
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Mutations in KIF5A are involved in hereditary spastic paraplegia<ref>PMID:18203753</ref>. Mutation in KIF1B is the cause of Charcot-Marie-Tooth disease <ref>PMID:14559185</ref>.
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Mutations in KIF5A are involved in hereditary spastic paraplegia<ref>PMID:18203753</ref>. Mutation in KIF1B is the cause of Charcot-Marie-Tooth disease <ref>PMID:14559185</ref>. Mutations in KIF22 cause spondyloepimetaphyseal dysplasia<ref>PMID:23665482</ref>.
== Structural highlights ==
== Structural highlights ==
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Residue Arg216 is the key residue in KIF for the chemical cycling of ATPase and for the mechanical cycling. Arg216 pivots to enable Mg-ADP release or the phosphate release. Arg216 forms a latch in the KIF 'closed-state' before the Mg-ADP release. Binding of β-tubulin to KIF releases the latch, enabling the KIF conformation change and detaching KIF from the microtubule and enabling the next movement cycle<ref>PMID:18806800</ref>.
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<scene name='41/410296/Cv/10'>Active site</scene>. Water molecules shown as red spheres. Residue <scene name='41/410296/Cv/11'>Arg216 is the key residue in KIF for the chemical cycling of ATPase and for the mechanical cycling</scene>. Arg216 pivots to enable <scene name='41/410296/Cv/12'>Mg-ADP</scene> release or the phosphate release. <scene name='41/410296/Cv/13'>Arg216 forms a latch</scene> in the KIF 'closed-state' before the Mg-ADP release. Binding of β-tubulin to KIF releases the latch, enabling the KIF conformation change and detaching KIF from the microtubule and enabling the next movement cycle<ref>PMID:18806800</ref>.
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<scene name='41/410296/Cv/14'>Mg coordination site</scene>.
== 3D Structures of Kinesin ==
== 3D Structures of Kinesin ==
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[[Kinesin 3D Structures]]
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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</StructureSection>
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{{#tree:id=OrganizedByTopic|openlevels=0|
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*Kinesin heavy chain
 
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**[[2zfi]], [[2zfj]], [[2zfk]], [[2zfl]], [[2zfm]] – mKIF1A – mouse<br />
 
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**[[2vvg]] – KIF2 MD – ''Giardia intestinalis''<br />
 
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**[[2g1l]] - hKIF1C FHA domain<br />
 
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**[[2owm]] – NcKIF1C MD – ''Neurospora crassa''<br />
 
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**[[1goj]] – NcKIF MD<br />
 
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**[[3bfn]] – hKIF22 MD<br />
 
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**[[3b6u]], [[3b6v]] – hKIF3B MD<br />
 
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**[[2rep]] – hKIFC1 MD<br />
 
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**[[2eh0]] - hKIF1B FHA domain – NMR<br />
 
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**[[2edu]] – hKIF22 C-terminal – NMR<br />
 
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**[[2v14]] – hKIF16B<br />
 
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**[[2heh]] – hKIF2C<br />
 
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**[[2cow]] – hKIF13B CAP-gly domain – NMR<br />
 
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**[[1bg2]] – hKIF MD<br />
 
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**[[3kin]], [[2kin]] – rKIF MD - rat<br />
 
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**[[1ry6]] – KIF MD – ''Plasmodium falciparum''<br />
 
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**[[2ncd]], [[1cz7]] – DmKIF MD non-claret disjuctional (NCD) dimer – ''Drosophila melanogaster'' <br />
 
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**[[2y5w]], [[2y65]] - DmKIF MD<br />
 
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*''Kinesin heavy chain complex with nucleotide''
 
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**[[3gbj]] – hKIF13B MD+ADP – human<br />
 
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**[[1vfv]], [[1vfw]] – mKIF1A MD+Mg-AMPPNP<br />
 
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**[[1vfx]] - mKIF1A MD+ADP-Mg-AlFx<br />
 
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**[[1vfz]] - mKIF1A MD+ADP-Mg-VO4<br />
 
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**[[1v8j]] – mKIF2C MD+Mg-ADP<br />
 
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**[[1i5s]] - mKIF2C MD (mutant)+Mg-ADP<br />
 
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**[[1i6i]] - mKIF2C MD (mutant)+Mg-AMPPCP<br />
 
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**[[1v8k]] - mKIF2C MD+Mg-AMPPNP<br />
 
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**[[3zfc]], [[3zfd]] – mKIF4 MD+Mg-AMPPNP<br />
 
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**[[2cjo]] – hKIF13+inhibitor 30<br />
 
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**[[2nr8]] – hKIF9+ADP<br />
 
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**[[2h58]] – hKIFC3+ADP<br />
 
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**[[2gry]] – hKIF2+ADP<br />
 
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**[[2hfx]] – pKIF1A head+AMPPNP – pig<br />
 
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**[[2hxh]] - pKIF1A head+ADP<br />
 
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*''Kinesin heavy chain complex with protein''
 
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**[[2wbe]] – cKIF MD+FNL+Tubulin A+Tubulin B+AMPPNP – cow <br />
 
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**[[1ia0]] – KIF1A MD+Tubulin A+Tubulin B+ATP - pig<br />
 
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**[[3edl]] – cKIF MD+ Tubulin A+Tubulin B – EM<br />
 
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**[[4hna]] – hKIF1 + Tubulin A + Tubulin B + designed ankyrin repeat protein + Mg-ADP + GDP + GTP + AlF4<br />
 
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**[[2p4n]] – hKIF+ Tubulin A+Tubulin B – EM docking<br />
 
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**[[1mkj]] – hKIF MD+docked FNL<br />
 
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**[[1n6m]] – DmKIF MD+FNL<br />
 
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**[[4atx]] - rKIF MD+ Tubulin A+Tubulin B – EM
 
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*Kinesin light chain (KLC)
 
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**[[3edt]] – hKLC2<br />
 
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**[[3ceq]], [[3nf1]] – hKLC2 TPR domain<br />
 
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**[[3zfw]] - mKLC2 TPR domain + peptide<br />
 
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*Kinesin-5 motor domain
 
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**[[4b7b]] - hKIF11 (mutant) + ADP + Co + Cd <br />
 
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**[[3ken]], [[2wog]], [[2x2r]], [[2xae]], [[4bbg]] - hKIF11 +S-trityl-L-cysteine derivative + ADP + Mg<br />
 
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**[[2uyi]], [[2uym]], [[2gm1]], [[2pg2]], [[2fme]], [[2x7d]], [[2x7c]], [[2ieh]], [[3cjo]], [[2g1q]], [[2fl2]], [[2fl6]], [[1yrs]], [[2q2y]], [[2fky]], [[2q2z]], [[3k3b]], [[2x7e]], [[4a50]], [[4a51]], [[3zcw]] - hKIF11+inhibitor +ADP + Mg<br />
 
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**[[4bxn]] - hKIF11+inhibitor +ADP + Cd<br />
 
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**[[3l9h]] - hKIF11+inhibitor +ADP <br />
 
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**[[1x88]], [[1q0b]] - hKIF11 +Mg + ADP+monastrol <br />
 
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**[[4ap0]], [[4a5y]] - hKIF11 +MgADP + ispinesib + Mg<br />
 
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**[[3hqd]] - hKIF11 +AMPPNP+Mg<br />
 
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**[[1ii6]], [[4a1z]], [[4a28]] - hKIF11 +ADP+Mg<br />
 
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**[[3k5e]] - hKIF11 +ADP+enastrol + Mg<br />
 
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**[[4aqv]], [[4aqw]] – hKIF11 (mutant) + tubulin + GDP + GTP + Mg – Cryo EM<br />
 
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**[[4ck5]], [[4ck6]], [[4ck7]] – hKIF11 (mutant) + tubulin + ADP + GDP + GTP + Mg – Cryo EM<br />
 
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*Kinesin-14
 
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**[[1f9t]], [[1f9u]], [[1f9v]], [[1f9w]], [[3kar]] - Kar3 MD (mutant) - yeast<br />
 
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**[[3l1c]] – DmNCD (mutant)
 
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*NOD
 
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**[[3dc4]] – DmNOD catalytic core domain+ADP<br />
 
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**[[3dcb]] - DmNOD catalytic core domain+AMPPNP<br />
 
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**[[3dco]] - DmNOD catalytic core domain+ cTubulin A+cTubulin B<br />
 
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}}
 
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

KIF1A Motor Domain complex with ADP and Mg+2 ion (green), 2zfi

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References

  1. ↑ Hirokawa N, Noda Y, Tanaka Y, Niwa S. Kinesin superfamily motor proteins and intracellular transport. Nat Rev Mol Cell Biol. 2009 Oct;10(10):682-96. doi: 10.1038/nrm2774. PMID:19773780 doi:http://dx.doi.org/10.1038/nrm2774
  2. ↑ Ebbing B, Mann K, Starosta A, Jaud J, Schols L, Schule R, Woehlke G. Effect of spastic paraplegia mutations in KIF5A kinesin on transport activity. Hum Mol Genet. 2008 May 1;17(9):1245-52. doi: 10.1093/hmg/ddn014. Epub 2008 Jan, 18. PMID:18203753 doi:http://dx.doi.org/10.1093/hmg/ddn014
  3. ↑ Hirokawa N, Takemura R. Biochemical and molecular characterization of diseases linked to motor proteins. Trends Biochem Sci. 2003 Oct;28(10):558-65. PMID:14559185 doi:http://dx.doi.org/10.1016/j.tibs.2003.08.006
  4. ↑ Grosch M, Gruner B, Spranger S, Stutz AM, Rausch T, Korbel JO, Seelow D, Nurnberg P, Sticht H, Lausch E, Zabel B, Winterpacht A, Tagariello A. Identification of a Ninein (NIN) mutation in a family with spondyloepimetaphyseal dysplasia with joint laxity (leptodactylic type)-like phenotype. Matrix Biol. 2013 Oct-Nov;32(7-8):387-92. doi: 10.1016/j.matbio.2013.05.001. Epub, 2013 May 9. PMID:23665482 doi:http://dx.doi.org/10.1016/j.matbio.2013.05.001
  5. ↑ Nitta R, Okada Y, Hirokawa N. Structural model for strain-dependent microtubule activation of Mg-ADP release from kinesin. Nat Struct Mol Biol. 2008 Oct;15(10):1067-75. Epub 2008 Sep 21. PMID:18806800 doi:10.1038/nsmb.1487
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