3J8Y

High-resolution structure of ATP analog-bound kinesin on microtubules

Summary for 3J8Y

• Entry DOI: 10.2210/pdb3j8y/pdb
• Related: 3J8X
• EMDB information: 6187 6188
• Descriptor: Kinesin-1 heavy chain, Tubulin alpha-1B chain, Tubulin beta-2B chain, ... (7 entities in total)
• Functional Keywords: molecular motors, kinesin, myosin, microtubules, cytoskeletal motors, motor protein-structural protein complex, motor protein/structural protein
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 3
• Total formula weight: 140924.28

Authors

Shang, Z.,Zhou, K.,Xu, C.,Csencsits, R.,Cochran, J.C.,Sindelar, C.V. (deposition date: 2014-11-20, release date: 2014-12-10, Last modification date: 2024-02-21)

Primary citation

Shang, Z.,Zhou, K.,Xu, C.,Csencsits, R.,Cochran, J.C.,Sindelar, C.V.
High-resolution structures of kinesin on microtubules provide a basis for nucleotide-gated force-generation.
Elife, 3:e04686-e04686, 2014

PubMed Abstract: Microtubule-based transport by the kinesin motors, powered by ATP hydrolysis, is essential for a wide range of vital processes in eukaryotes. We obtained insight into this process by developing atomic models for no-nucleotide and ATP states of the monomeric kinesin motor domain on microtubules from cryo-EM reconstructions at 5-6 Å resolution. By comparing these models with existing X-ray structures of ADP-bound kinesin, we infer a mechanistic scheme in which microtubule attachment, mediated by a universally conserved 'linchpin' residue in kinesin (N255), triggers a clamshell opening of the nucleotide cleft and accompanying release of ADP. Binding of ATP re-closes the cleft in a manner that tightly couples to translocation of cargo, via kinesin's 'neck linker' element. These structural transitions are reminiscent of the analogous nucleotide-exchange steps in the myosin and F1-ATPase motors and inform how the two heads of a kinesin dimer 'gate' each other to promote coordinated stepping along microtubules.

PubMed: 25415053
DOI: 10.7554/eLife.04686

Experimental method

ELECTRON MICROSCOPY (5 Å)