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Kinesins second step
Kinesin's second step.
18
We have identified dimeric kinesin mutants that become stalled on the microtubule after one ATP turnover, unable to bind and hydrolyze ATP at their second site. We have used these mutants to determine the regulatory signal that allows ATP to bind to the forward head, such that processive movement can continue. The results show that phosphate release occurs from the rearward head before detachment, and detachment triggers active-site accessibility for ATP binding at the forward head. This mechanism, in which the rearward head controls the behavior of the forward head, may be conserved among processive motors.
Klumpp LM, Hoenger A, Gilbert SP
Proceedings of the National Academy of Sciences of the United States of America
2004-03-09 00:00
101
10
3444-9
Adenosine Triphosphate,Animals,Dimerization,Drosophila Proteins,Drosophila melanogaster,Humans,Kinesin,Kinetics,Macromolecular Substances,Microtubules,Models, Biological,Models, Molecular,Molecular Motor Proteins,Mutagenesis, Site-Directed,Rats,Drosophila Proteins,Macromolecular Substances,Molecular Motor Proteins,Adenosine Triphosphate,Kinesin
Department of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260, USA
Proc. Natl. Acad. Sci. U.S.A.
NIGMS GM54141, NIAMS K02-AR47841
0027-8424
10.1073/pnas.0307691101
0307691101
560
True
14985504
