High-resolution structures of kinesin on microtubules provide a basis for nucleotide-gated force-generation

Shang, Zhiguo; Zhou, Kaifeng; Xu, Chen; Csencsits, Roseann; Cochran, Jared C.; Sindelar, Charles V.

doi:10.7554/elife.04686

High-resolution structures of kinesin on microtubules provide a basis for nucleotide-gated force-generation

Journal Article · Fri Nov 21 04:00:00 EST 2014 · eLife

DOI:https://doi.org/10.7554/elife.04686· OSTI ID:1628826

Shang, Zhiguo ^[1]; Zhou, Kaifeng ^[2]; Xu, Chen ^[3]; Csencsits, Roseann ^[4]; Cochran, Jared C. ^[5]; Sindelar, Charles V. ^[2]

Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, United States; DOE/OSTI
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, United States
Department of Biology, Brandeis University, Waltham, United States
Life Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, United States
Department of Molecular and Cellular Biochemistry, Indiana University, Bloomington, United States

Microtubule-based transport by the kinesin motors, powered by ATP hydrolysis, is essential for a wide range of vital processes in eukaryotes. We obtained insight into this process by developing atomic models for no-nucleotide and ATP states of the monomeric kinesin motor domain on microtubules from cryo-EM reconstructions at 5–6 Å resolution. By comparing these models with existing X-ray structures of ADP-bound kinesin, we infer a mechanistic scheme in which microtubule attachment, mediated by a universally conserved ‘linchpin’ residue in kinesin (N255), triggers a clamshell opening of the nucleotide cleft and accompanying release of ADP. Binding of ATP re-closes the cleft in a manner that tightly couples to translocation of cargo, via kinesin's ‘neck linker’ element. These structural transitions are reminiscent of the analogous nucleotide-exchange steps in the myosin and F1-ATPase motors and inform how the two heads of a kinesin dimer ‘gate’ each other to promote coordinated stepping along microtubules.

View Accepted Manuscript (DOE)

Research Organization:: Lawrence Berkeley National Lab (LBNL), Berkeley, CA (United States)

Sponsoring Organization:: USDOE Office of Science (SC); American Cancer Society; National Institutes of Health

Grant/Contract Number:: AC02-05CH11231

OSTI ID:: 1628826

Journal Information:: eLife, Journal Name: eLife Vol. 3; ISSN 2050-084X

Publisher:: eLife Sciences Publications, Ltd.Copyright Statement

Country of Publication:: United States

Language:: English

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