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The structure of apo-kinesin bound to tubulin links the nucleotide cycle to movement
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The structure of apo-kinesin bound to tubulin links the nucleotide cycle to movement
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Journal Article
The structure of apo-kinesin bound to tubulin links the nucleotide cycle to movement
2014
Overview
Kinesin-1 is a dimeric ATP-dependent motor protein that moves towards microtubules (+) ends. This movement is driven by two conformations (docked and undocked) of the two motor domains carboxy-terminal peptides (named neck linkers), in correlation with the nucleotide bound to each motor domain. Despite extensive data on kinesin-1, the structural connection between its nucleotide cycle and movement has remained elusive, mostly because the structure of the critical tubulin-bound apo-kinesin state was unknown. Here we report the 2.2 Å structure of this complex. From its comparison with detached kinesin–ADP and tubulin-bound kinesin–ATP, we identify three kinesin motor subdomains that move rigidly along the nucleotide cycle. Our data reveal how these subdomains reorient on binding to tubulin and when ATP binds, leading respectively to ADP release and to neck linker docking. These results establish a framework for understanding the transformation of chemical energy into mechanical work by (+) end-directed kinesins.
A complete description of how the motor protein kinesin-1 walks along microtubules is missing because of the lack of a key structure. Here, Cao
et al
. solve the apo-kinesin:microtubule structure, completing the structure set and permitting the description of the structural changes that occur during the nucleotide cycle and their functional consequences.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 82
/ Adenosine Triphosphatases - metabolism
/ Adenosine Triphosphatases - physiology
/ Adenosine Triphosphate - metabolism
/ Adenosine Triphosphate - physiology
/ ATP
/ Biochemistry, Molecular Biology
/ Humanities and Social Sciences
/ Humans
/ Molecular Docking Simulation
/ Peptides
/ Protein Structure, Tertiary - physiology
/ Science
