4LNU

Nucleotide-free kinesin motor domain in complex with tubulin and a DARPin

Summary for 4LNU

• Entry DOI: 10.2210/pdb4lnu/pdb
• Descriptor: Tubulin alpha chain, GLYCEROL, Tubulin beta chain, ... (11 entities in total)
• Functional Keywords: alpha-tubulin, apo-kinesin, beta-tubulin, darpin, kinesin, microtubule, tubulin, cell cycle-motor protein complex, cell cycle/motor protein
• Biological source: Artificial gene; More
• Cellular location: Cytoplasm, cytoskeleton : P33176
• Total number of polymer chains: 4
• Total formula weight: 157232.55

Authors

Cao, L.,Gigant, B.,Knossow, M. (deposition date: 2013-07-12, release date: 2014-12-03, Last modification date: 2023-11-08)

Primary citation

Cao, L.,Wang, W.,Jiang, Q.,Wang, C.,Knossow, M.,Gigant, B.
The structure of apo-kinesin bound to tubulin links the nucleotide cycle to movement
Nat Commun, 5:5364-5364, 2014

PubMed 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.

PubMed: 25395082
DOI: 10.1038/ncomms6364

Experimental method

X-RAY DIFFRACTION (2.19 Å)