Kinesin

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[[Image:Kif1A Motor Domain.jpg|left|200px]]<br />
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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]]'>
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<applet load="2zfi.pdb" size="300" color="white" frame="true" spin="on" caption="Kinesin" align="right"/>
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== Function ==
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'''3D Structure of Kinesin'''<br />
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== Kinesin ==
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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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Kinesins are eukaryotic motor proteins which move along microtubules. Kinesin (KIF) is a dimer consisting of 2 heavy chains and two light chains. The heavy chain contains the globular motor domain (MD), flexible neck linker (FNL) and a long coiled-coil stalk which intertwines to form the dimer. 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. Kinesin protein in yeast is called Kar3. Eg5 or KIF11 is a kinesin which participates in mitosis. KCBP is a Kinesin-like Calmodulin Binding Protein. NOD is a Drosophila chromosome-associated kinesin.
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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 />
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*'''Kar3''' is kinesin protein in yeast.<br />
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*'''Eg5''' or '''KIF11''' is a kinesin (See [[Kinesin-5]]) which participates in mitosis.<br />
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*'''NOD''' is a ''Drosophila'' chromosome-associated kinesin.
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See also [[CAP-Gly domain]].
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== 3D Structures of Kinesin ==
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== 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>. Mutations in KIF22 cause spondyloepimetaphyseal dysplasia<ref>PMID:23665482</ref>.
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===Kinesin Heavy Chain (KIF)===
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== Structural highlights ==
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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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[[3hog]] – SOD – tomato <br />
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<scene name='41/410296/Cv/14'>Mg coordination site</scene>.
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[[1p7g]] – SOD – Pyrobaculum aerophilum <br />
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== 3D Structures of Kinesin ==
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[[Kinesin 3D Structures]]
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===Cu-Zn-SOD===
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[[2jlp]], [[2v0a]], [[2c9v]], [[2c9u]], [[2c9s]], [[1pu0]], [[1hl5]], [[1sos]], [[1spd]] - hSOD +Zn+Cu - human<br />
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[[3h2p]], [[3h2q]], [[3h2r]], [[3hff]], [[3gqf]], [[2nnx]], [[1p1v]], [[1oez]] – hSOD (mutant) +Zn<br />
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[[2af2]], [[1kmg]] - hSOD (mutant) +Zn – NMR<br />
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[[1l3n]], [[1dsw]], [[1ba9]] – hSOD (mutant) +Zn+Cu - NMR<br />
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[[1rk7]] - hSOD (mutant) apo – NMR<br />
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[[1ozt]], [[3gzp]], [[3gzq]], [[3ecv]], [[3ecw]], [[2gbu]] - hSOD (mutant) apo<br />
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[[3ecu]], [[3k91]] – hSOD apo<br />
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[[2r27]] - hSOD +Cu<br />
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[[1hl4]] - hSOD +Zn<br />
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[[2wko]], [[3gzo]],[[ 2zkw]], [[2zkx]], [[2zky]], [[3cqp]], [[3cqq]], [[2vr6]], [[2vr7]], [[2vr8]], [[2gbt]], [[2gbv]], [[1uxl]], [[1uxm]], [[1ptz]], [[1ozu]], [[1n18]], [[1n19]], [[1fun]], [[1mfm]], [[1azv]] – hSOD (mutant) +Zn+Cu<br />
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[[3l9e]] - smSOD +Zn – silk moth<br />
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[[3l9y]] - smSOD +Zn+Cu<br />
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[[2wn0]] – YpSOD+Zn+Cu – Yersinia pseudotuberculosis<br />
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[[2wn1]] - YpSOD+Zn+Cu+N3<br />
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[[2z7u]], [[2z7w]], [[2z7y]], [[2z7z]], [[2aeo]], [[1q0e]], [[1e9p]], [[1e9q]], [[1cb4]], [[1cbj]], [[1sxn]], [[1sxa]], [[1sxb]], [[1sxc]], [[1spd]], [[1sda]], [[3sod]], [[2sod]], [[2zow]], [[3hw7]] – cSOD+Zn+Cu - cow<br />
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[[1cob]] – cSOD+Cu+Co<br />
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[[1sxs]] - cSOD +Zn+Cu+SCN<br />
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[[1sxz]] - cSOD +Zn+Cu+N3<br />
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[[1e9o]] – cSOD+Cu<br />
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[[3f7k]] - ApSOD +Zn+Cu+H2O2 – Alvinella pompejana<br />
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[[3f7l]] - ApSOD +Zn+Cu<br />
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[[2k4w]] – SeSOD (mutant) +Zn+Cu – Salmonella enterica – NMR<br />
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[[1eqw]] - SOD +Zn+Cu – Salmonella typhimurium<br />
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[[3ce1]] - SOD +Zn+Cu – Cryptococcus liquefaciens<br />
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[[2q2l]] - SOD +Zn – Potentilla atrosanguinea<br />
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[[2aqm]] - SOD +Zn+Cu – Brucella abortus<br />
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[[2aps]] - SOD +Zn+Cu – Actinobacillus pleuropneumoniae<br />
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[[2aqn]] - NmSOD +Zn+Cu – Neisseria meningitides<br />
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[[2aqp]], [[2aqq]], [[2aqr]], [[2aqs]], [[2aqt]] – NmSOD (mutant) +Zn+Cu<br />
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[[1z9n]] - HdSOD +Zn+Cu+haem – Haemophilus ducreyi<br />
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[[1z9p]] - HdSOD +Zn+Cu<br />
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[[1to4]], [[1to5]] - SOD +Zn+Cu – Schistosoma mansoni<br />
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[[1pzs]] - MtSOD +Cu – Mycobacterium tuberculosis<br />
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[[1oaj]], [[1bzo]], [[1yai]] - PlSOD +Zn+Cu – Photobacterium leiognathi<br />
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[[1oal]], [[1ib5]], [[1ibb]], [[1ibd]], [[1ibf]], [[1ibh]] – PlSOD (mutant) +Zn+Cu<br />
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[[1f18]], [[1f1a]], [[1f1d]], [[1b4t]] – ySOD (mutant) +Zn+Cu – yeast<br />
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[[1f1g]], [[1b4l]], [[2jcw]], [[1sdy]] - ySOD +Zn+Cu<br />
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[[1yaz]] - ySOD +Zn+Cu+N3<br />
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[[1jk9]] – ySOD+Zn+Cu chaperone for SOD<br />
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[[1eso]] - EcSOD +Zn+Cu - Escherichia coli<br />
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[[1yso]] - EcSOD +Zn+Cu<br />
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[[1srd]] – SOD+MZn+Cu –Spinach<br />
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===Mn-SOD===
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[[3k9s]] – EcSOD+H2O2 <br />
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[[1d5n]], [[1vew]] - EcSOD+Mn<br />
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[[1mmm]] – EcSOD+Fe<br />
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[[1zlz]], [[1ixb]], [[1ix9]], [[1en4]], [[1en5]], [[1en6]], [[1i08]], [[1i0h]] – EcSOD (mutant)+Mn<br />
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[[3dc5]], [[3dc6]] – SOD+Mn – Caenorhabditis elegans<br />
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[[3bfr]], [[1jcv]] – ySOD+Mn <br />
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[[2qka]], [[2adp]], [[2adq]], [[1xdc]], [[1xil]], [[1n0j]], [[1luv]], [[1msd]] – hSOD+Mn<br />
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[[2qkc]], [[3c3s]], [[3c3t]], [[2p4k]], [[1zsp]], [[1zte]], [[1zuq]], [[2gds]], [[1szx]], [[1pl4]], [[1pm9]], [[1n0n]], [[1luw]], [[1ja8]], [[1em1]], [[1ap5]], [[1ap6]], [[1qnm]], [[1var]] – hSOD (mutant)+Mn<br />
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[[2rcv]] – SOD+Mn – Bacillus subtilis<br />
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[[1xre]], [[1xuq]] – SOD+Mn – Bacillus anthracis<br />
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[[2aw9]], [[2cdy]], [[2ce4]] – DrSOD+Mn – Deinococcus radiodurans<br />
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[[1y67]] – DrSOD+Fe<br />
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[[2a03]] – SOD+Mn+Zn – Plasmodium berghei<br />
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[[1jr9]] - SOD +Zn+Mn – Virgibacillus halodenitrificans<br />
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[[1gv3]] – SOD+Mn – Anabaena<br />
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[[1kkc]] – SOD+Mn – Aspergillus fumigatus<br />
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[[1xso]] – SOD+Mn – Xenopus laevis<br />
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[[1mng]], [[3mds]] – TtSOD+Mn – Thermus thermophilus<br />
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===Fe-SOD===
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[[3js4]] – SOD+Fe – Anaplasma phagocytuphilum<br />
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[[3evk]] – SOD+Mn – Pyrobaculum aerophilum<br />
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[[3esf]] – SOD (mutant)+Fe – Trypanosoma brucei<br />
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[[2gpc]] – SOD+Fe – Trypanosoma cruzi<br />
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[[3h1s]] – SOD+Fe – Francisella tularensis<br />
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[[2w7w]] – SOD+Fe – Aliivibrio salmonicida<br />
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[[3cei]] – SOD+Fe – Helicobacter pylori<br />
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[[2goj]], [[2bpi]] – PfSOD+Fe – Plasmodium falciparum<br />
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[[2awp]] – SOD+ion – Plasmodium knowlesi<br />
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[[2bkb]], [[2nyb]], [[1za5]] – EcSOD (mutant)+Fe<br />
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[[2cw2]], [[2cw3]] – SOD+Fe – Perkinsus marinus<br />
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[[1wb7]], [[1wb8]] – SOD (mutant)+Fe – Sulfolobus solfataricus<br />
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[[1unf]] – SOD+Fe – Vigna unguiculata<br />
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[[1uer]], [[1ues]], [[1qnn]] – SOD+Fe – Porphyromonas gingivalis<br />
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[[1my6]] – SOD+Fe – Thermosynechococcus elongates<br />
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[[1ma1]] – SOD+Fe – Methanothermobacter thermautotrophicus<br />
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[[1gn2]], [[1gn3]], [[1gn4]], [[1gn6]] – MtSOD (mutant)+Fe<br />
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[[1ids]] – MtSOD+Fe<br />
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[[1dt0]], [[3sdp]] – SOD+Fe – Pseudomonas putida<br />
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[[1b06]] – SOD+Fe – Sulfolobus acidocaldarius<br />
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[[1bs3]] – PfSOD+Fe+F – Propionibacterium freudenreichii<br />
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[[1bsm]], [[1bt8]] – PfSOD+Fe<br />
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[[1ar4]], [[1ar5]] – PfSOD+Mn<br />
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[[1avm]] – PfSOD+Fe+N3<br />
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[[1coj]] – SOD+Fe – Aquifex pyrophilus<br />
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[[1isa]], [[1isb]], [[1isc]] – EcSOD+Fe <br />
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</StructureSection>
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===Ni-SOD===
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== References ==
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[[3g4x]], [[3g4z]], [[3g50]], [[1t6u]] – ScSOD (mutant)+Ni – Streptomyces coelicolor<br />
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<references/>
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[[1t6i]], [[1t6q]] – ScSOD apo <br />
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[[Category:Topic Page]]
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[[1q0d]], [[1q0f]], [[1q0g]], [[1q0k]], [[1q0m]] – SOD+Ni – Streptomyces seoulensis<br />
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Current revision

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

Drag the structure with the mouse to rotate

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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