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TitleStructural basis of cooperativity in kinesin revealed by 3D reconstruction of a two-head-bound state on microtubules.
Journal, issue, pagesElife, Vol. 6, Year 2017
Publish dateMay 15, 2017
AuthorsDaifei Liu / Xueqi Liu / Zhiguo Shang / Charles V Sindelar /
PubMed AbstractThe detailed basis of walking by dimeric molecules of kinesin along microtubules has remained unclear, partly because available structural methods have been unable to capture microtubule-bound ...The detailed basis of walking by dimeric molecules of kinesin along microtubules has remained unclear, partly because available structural methods have been unable to capture microtubule-bound intermediates of this process. Utilizing novel electron cryomicroscopy methods, we solved structures of microtubule-attached, dimeric kinesin bound to an ATP analog. We find that under these conditions, the kinesin dimer can attach to the microtubule with either one or two motor domains, and we present sub-nanometer resolution reconstructions of both states. The former structure reveals a novel kinesin conformation that revises the current understanding of how ATP binding is coupled to forward stepping of the motor. The latter structure indicates how tension between the two motor domains keeps their cycles out of phase in order to stimulate directional motility. The methods presented here pave the way for future structural studies of a variety of challenging macromolecules that bind to microtubules and other filaments.
External linksElife / PubMed:28504639 / PubMed Central
MethodsEM (single particle)
Resolution6.7 - 7.3 Å
Structure data

EMDB-8546:
Dimeric Kinesin-1 on Microtubules with ADP-AlFx
Method: EM (single particle) / Resolution: 7.3 Å

EMDB-8547:
Kinesin-1 Binding Microtubules with ADP-AlFx in a One-head-bound State (low-pass filtered to 8.5 angstrom)
Method: EM (single particle) / Resolution: 6.7 Å

Source
  • Bos taurus (cattle)
  • Homo sapiens (human)

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