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

doi:10.1126/science.1082374

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

Cell & Developmental Biology

Research output: Contribution to journal › Article › peer-review

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 language	English (US)
Pages (from-to)	798-801
Number of pages	4
Journal	Science
Volume	300
Issue number	5620
DOIs	https://doi.org/10.1126/science.1082374
State	Published - May 2 2003

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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.",

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T1 - Closing of the nucleotide pocket of kinesin-family motors upon binding to microtubules

AU - Naber, Nariman

AU - Minehardt, Todd J.

AU - Rice, Sarah

AU - Chen, Xiaoru

AU - Grammer, Jean

AU - Matuska, Marija

AU - Vale, Ronald D.

AU - Kollman, Peter A.

AU - Car, Roberto

AU - Yount, Ralph G.

AU - Cooke, Roger

AU - Pate, Edward

PY - 2003/5/2

Y1 - 2003/5/2

N2 - 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.

AB - 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.

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

Abstract

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