Magic-angle-spinning NMR structure of the kinesin-1 motor domain assembled with microtubules reveals the elusive neck linker orientation

Chunting Zhang; Changmiao Guo; Ryan W. Russell; Caitlin M. Quinn; Mingyue Li; John C. Williams; Angela M. Gronenborn; Tatyana Polenova

doi:10.1038/s41467-022-34026-w

Nature Communications (Nov 2022)

Magic-angle-spinning NMR structure of the kinesin-1 motor domain assembled with microtubules reveals the elusive neck linker orientation

Chunting Zhang,
Changmiao Guo,
Ryan W. Russell,
Caitlin M. Quinn,
Mingyue Li,
John C. Williams,
Angela M. Gronenborn,
Tatyana Polenova

Affiliations

Chunting Zhang: Department of Chemistry and Biochemistry, University of Delaware
Changmiao Guo: Department of Chemistry and Biochemistry, University of Delaware
Ryan W. Russell: Department of Chemistry and Biochemistry, University of Delaware
Caitlin M. Quinn: Department of Chemistry and Biochemistry, University of Delaware
Mingyue Li: Department of Chemistry and Biochemistry, University of Delaware
John C. Williams: Department of Molecular Medicine, Beckman Research Institute of City of Hope
Angela M. Gronenborn: Department of Structural Biology, University of Pittsburgh School of Medicine
Tatyana Polenova: Department of Chemistry and Biochemistry, University of Delaware

DOI: https://doi.org/10.1038/s41467-022-34026-w
Journal volume & issue: Vol. 13, no. 1
pp. 1 – 12

Abstract

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In this work the authors report the structure of nucleotide-free kinesin-1 motor domain (apo-KIF5B) in complex with paclitaxel-stabilized microtubules using magic-angle-spinning (MAS) NMR spectroscopy. The study provides insights into the dynamic changes under which the neck linker goes upon binding to ADP.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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