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5ND7

Microtubule-bound MKLP2 motor domain in the presence of AMPPNP

Summary for 5ND7
Entry DOI10.2210/pdb5nd7/pdb
EMDB information3623
DescriptorKinesin-like protein KIF20A, Tubulin alpha chain, Tubulin beta-2B chain, ... (8 entities in total)
Functional Keywordskinesin mitosis microtubules, motor protein
Biological sourceMus musculus (House Mouse)
More
Cellular locationGolgi apparatus : P97329
Cytoplasm, cytoskeleton : F2Z4C1 Q6B856
Total number of polymer chains3
Total formula weight158411.43
Authors
Primary citationAtherton, 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: 28826477
DOI: 10.7554/eLife.27793
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (7.9 Å)
Structure validation

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