3kin

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KINESIN (DIMERIC) FROM RATTUS NORVEGICUSKINESIN (DIMERIC) FROM RATTUS NORVEGICUS

Structural highlights

3kin is a 4 chain structure with sequence from Rattus norvegicus. The April 2005 RCSB PDB Molecule of the Month feature on Kinesin by David S. Goodsell is 10.2210/rcsb_pdb/mom_2005_4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.1Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

KIF5C_RAT Microtubule-associated force-producing protein that may play a role in organelle transport (By similarity). Has ATPase activity (PubMed:27452403). Involved in synaptic transmission (By similarity). Mediates dendritic trafficking of mRNAs (By similarity). Required for anterograde axonal transportation of MAPK8IP3/JIP3 which is essential for MAPK8IP3/JIP3 function in axon elongation (PubMed:23576431).[UniProtKB:O60282][UniProtKB:P28738][1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The dimeric form of the kinesin motor and neck domain from rat brain with bound ADP has been solved by X-ray crystallography. The two heads of the dimer are connected via a coiled-coil alpha-helical interaction of their necks. They are broadly similar to one another; differences are most apparent in the head-neck junction and in a moderate reorientation of the neck helices in order to adopt to the coiled-coil conformation. The heads show a rotational symmetry (approximately 120 degrees) about an axis close to that of the coiled-coil. This arrangement is unexpected since it is not compatible with the microtubule lattice. In this arrangement, the two heads of a kinesin dimer could not have equivalent interactions with microtubules.

The crystal structure of dimeric kinesin and implications for microtubule-dependent motility.,Kozielski F, Sack S, Marx A, Thormahlen M, Schonbrunn E, Biou V, Thompson A, Mandelkow EM, Mandelkow E Cell. 1997 Dec 26;91(7):985-94. PMID:9428521[3]

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

See Also

References

  1. ↑ Sun T, Yu N, Zhai LK, Li N, Zhang C, Zhou L, Huang Z, Jiang XY, Shen Y, Chen ZY. c-Jun NH2-terminal kinase (JNK)-interacting protein-3 (JIP3) regulates neuronal J Biol Chem. 2013 May 17;288(20):14531-14543. PMID:23576431 doi:10.1074/jbc.M113.464453
  2. ↑ Yamagishi M, Shigematsu H, Yokoyama T, Kikkawa M, Sugawa M, Aoki M, Shirouzu M, Yajima J, Nitta R. Structural Basis of Backwards Motion in Kinesin-1-Kinesin-14 Chimera: Implication for Kinesin-14 Motility. Structure. 2016 Aug 2;24(8):1322-34. doi: 10.1016/j.str.2016.05.021. Epub 2016, Jul 21. PMID:27452403 doi:http://dx.doi.org/10.1016/j.str.2016.05.021
  3. ↑ Kozielski F, Sack S, Marx A, Thormahlen M, Schonbrunn E, Biou V, Thompson A, Mandelkow EM, Mandelkow E. The crystal structure of dimeric kinesin and implications for microtubule-dependent motility. Cell. 1997 Dec 26;91(7):985-94. PMID:9428521

3kin, resolution 3.10Å

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