The structure of apo-kinesin bound to tubulin links the nucleotide cycle to movement

Luyan Cao, Weiyi Wang, Qiyang Jiang, Chunguang Wang (), Marcel Knossow () and Benoît Gigant ()
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Luyan Cao: Laboratoire d’Enzymologie et Biochimie Structurales (LEBS), Centre de Recherche de Gif, Centre National de la Recherche Scientifique
Weiyi Wang: Laboratoire d’Enzymologie et Biochimie Structurales (LEBS), Centre de Recherche de Gif, Centre National de la Recherche Scientifique
Qiyang Jiang: Institute of Protein Research, Tongji University
Chunguang Wang: Institute of Protein Research, Tongji University
Marcel Knossow: Laboratoire d’Enzymologie et Biochimie Structurales (LEBS), Centre de Recherche de Gif, Centre National de la Recherche Scientifique
Benoît Gigant: Laboratoire d’Enzymologie et Biochimie Structurales (LEBS), Centre de Recherche de Gif, Centre National de la Recherche Scientifique

Nature Communications, 2014, vol. 5, issue 1, 1-9

Abstract: Abstract 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.

Date: 2014
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DOI: 10.1038/ncomms6364

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