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J. Biol. Chem., Vol. 275, Issue 45, 35413-35423, November 10, 2000
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From the Departments of Although crystallographic information is
available on several nucleotide-induced states in myosin, little is
known about the corresponding structural changes in kinesin, since a
crystallographic model is only available for the kinesin:ADP complex.
This makes it difficult to characterize at a molecular level the
structural changes that occur in this motor through the course of its
ATPase cycle. In this study, we report on the production of a series of
single tryptophan mutants of a monomeric human kinesin motor domain,
which demonstrate nucleotide-dependent changes in microtubule affinity that are similar to wild type. We have used these mutations to
measure intramolecular distances in both strong and weak binding states, using florescence resonance energy transfer. This work provides
direct evidence that movement of the switch II loop and helix are
essential to mediate communication between the catalytic and
microtubule binding sites, evidence that is supported as well by
molecular modeling. Kinetic studies of fluorescent nucleotide binding
to these mutants are consistent with these distance changes, and
demonstrate as well that binding of ADP produces two structural transitions, neither of which are identical to that produced by the
binding of ATP. This study provides a basis for understanding current
structural models of the kinesin mechanochemical cycle.
Kinesin Has Three Nucleotide-dependent
Conformations
IMPLICATIONS FOR STRAIN-DEPENDENT RELEASE*
,
,, and Biochemistry and Molecular
Genetics and ¶ Neurology and the Graduate Program in Cell
and Molecular Biology, University of Alabama at Birmingham, Birmingham,
Alabama 35294 and the § Department of Molecular Biology,
Scripps Research Institute, La Jolla, California 92037
*
This work was supported by National Institutes of Health
Grant NS34856 (to S. S. R.) and Grant RR10404 (to H. C. C.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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