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© Research
Publication : The EMBO journal

Microscopic evidence for a minus-end-directed power stroke in the kinesin motor ncd.

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in The EMBO journal - 15 Nov 2002

Wendt TG, Volkmann N, Skiniotis G, Goldie KN, Müller J, Mandelkow E, Hoenger A,

Link to Pubmed [PMID] – 12426369

EMBO J 2002 Nov; 21(22): 5969-78

We used cryo-electron microscopy and image reconstruction to investigate the structure and microtubule-binding configurations of dimeric non-claret disjunctional (ncd) motor domains under various nucleotide conditions, and applied molecular docking using ncd’s dimeric X-ray structure to generate a mechanistic model for force transduction. To visualize the alpha-helical coiled-coil neck better, we engineered an SH3 domain to the N-terminal end of our ncd construct (296-700). Ncd exhibits strikingly different nucleotide-dependent three-dimensional conformations and microtubule-binding patterns from those of conventional kinesin. In the absence of nucleotide, the neck adapts a configuration close to that found in the X-ray structure with stable interactions between the neck and motor core domain. Minus-end-directed movement is based mainly on two key events: (i) the stable neck-core interactions in ncd generate a binding geometry between motor and microtubule which places the motor ahead of its cargo in the minus-end direction; and (ii) after the uptake of ATP, the two heads rearrange their position relative to each other in a way that promotes a swing of the neck in the minus-end direction.

https://pubmed.ncbi.nlm.nih.gov/12426369