Closing of the nucleotide pocket of kinesin-family motors upon binding to microtubules

Nariman Naber*, Todd J. Minehardt, Sarah Rice, Xiaoru Chen, Jean Grammer, Marija Matuska, Ronald D. Vale, Peter A. Kollman, Roberto Car, Ralph G. Yount, Roger Cooke, Edward Pate

*Corresponding author for this work

Research output: Contribution to journalArticle

50 Scopus citations

Abstract

We have used adenosine diphosphate analogs containing electron paramagnetic resonance (EPR) spin moieties and EPR spectroscopy to show that the nucleotide-binding site of kinesin-family motors closes when the motor-diphosphate complex binds to microtubules. Structural analyses demonstrate that a domain movement in the switch 1 region at the nucleotide site, homologous to domain movements in the switch 1 region in the G proteins [heterotrimeric guanine nucleotide-binding proteins], explains the EPR data. The switch movement primes the motor both for the free energy-yielding nucleotide hydrolysis reaction and for subsequent conformational changes that are crucial for the generation of force and directed motion along the microtubule.

Original languageEnglish (US)
Pages (from-to)798-801
Number of pages4
JournalScience
Volume300
Issue number5620
DOIs
StatePublished - May 2 2003

ASJC Scopus subject areas

  • General

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    Naber, N., Minehardt, T. J., Rice, S., Chen, X., Grammer, J., Matuska, M., Vale, R. D., Kollman, P. A., Car, R., Yount, R. G., Cooke, R., & Pate, E. (2003). Closing of the nucleotide pocket of kinesin-family motors upon binding to microtubules. Science, 300(5620), 798-801. https://doi.org/10.1126/science.1082374