Structural basis of cooperativity in kinesin revealed by 3D reconstruction of a two-head-bound state on microtubules.

ABSTRACT: 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

SUBMITTER: Liu D 

PROVIDER: S-EPMC5459574 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature