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Title | Microscopic evidence for a minus-end-directed power stroke in the kinesin motor ncd. |
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Journal, issue, pages | EMBO J, Vol. 21, Issue 22, Page 5969-5978, Year 2002 |
Publish date | Nov 15, 2002 |
Authors | Thomas G Wendt / Niels Volkmann / Georgios Skiniotis / Kenneth N Goldie / Jens Müller / Eckhard Mandelkow / Andreas Hoenger / |
PubMed Abstract | 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 ...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. |
External links | EMBO J / PubMed:12426369 / PubMed Central |
Methods | EM (helical sym.) |
Structure data | EMDB-1025: EMDB-1026: |
Source |
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