5ND7
Microtubule-bound MKLP2 motor domain in the presence of AMPPNP
Summary for 5ND7
Entry DOI | 10.2210/pdb5nd7/pdb |
EMDB information | 3623 |
Descriptor | Kinesin-like protein KIF20A, Tubulin alpha chain, Tubulin beta-2B chain, ... (8 entities in total) |
Functional Keywords | kinesin mitosis microtubules, motor protein |
Biological source | Mus musculus (House Mouse) More |
Cellular location | Golgi apparatus : P97329 Cytoplasm, cytoskeleton : F2Z4C1 Q6B856 |
Total number of polymer chains | 3 |
Total formula weight | 158411.43 |
Authors | Atherton, J.,Yu, I.-M.,Cook, A.,Muretta, J.M.,Joseph, A.P.,Major, J.,Sourigues, Y.,Clause, J.,Topf, M.,Rosenfeld, S.S.,Houdusse, A.,Moores, C.A. (deposition date: 2017-03-07, release date: 2017-10-04) |
Primary citation | Atherton, J.,Yu, I.M.,Cook, A.,Muretta, J.M.,Joseph, A.,Major, J.,Sourigues, Y.,Clause, J.,Topf, M.,Rosenfeld, S.S.,Houdusse, A.,Moores, C.A. The divergent mitotic kinesin MKLP2 exhibits atypical structure and mechanochemistry. Elife, 6:-, 2017 Cited by PubMed Abstract: MKLP2, a kinesin-6, has critical roles during the metaphase-anaphase transition and cytokinesis. Its motor domain contains conserved nucleotide binding motifs, but is divergent in sequence (~35% identity) and size (~40% larger) compared to other kinesins. Using cryo-electron microscopy and biophysical assays, we have undertaken a mechanochemical dissection of the microtubule-bound MKLP2 motor domain during its ATPase cycle, and show that many facets of its mechanism are distinct from other kinesins. While the MKLP2 neck-linker is directed towards the microtubule plus-end in an ATP-like state, it does not fully dock along the motor domain. Furthermore, the footprint of the MKLP2 motor domain on the MT surface is altered compared to motile kinesins, and enhanced by kinesin-6-specific sequences. The conformation of the highly extended loop6 insertion characteristic of kinesin-6s is nucleotide-independent and does not contact the MT surface. Our results emphasize the role of family-specific insertions in modulating kinesin motor function. PubMed: 28826477DOI: 10.7554/eLife.27793 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (7.9 Å) |
Structure validation
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