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Science. 2003 May 2;300(5620):798-801.

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

Author information

1
Department of Biochemistry, University of California, San Francisco, CA 94143, USA. naber@itsa.ucsf.edu

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.

PMID:
12730601
DOI:
10.1126/science.1082374
[Indexed for MEDLINE]
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