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| Title | The beginning of kinesin's force-generating cycle visualized at 9-A resolution. |
|---|---|
| Journal, issue, pages | J Cell Biol, Vol. 177, Issue 3, Page 377-385, Year 2007 |
| Publish date | May 7, 2007 |
Authors | Charles V Sindelar / Kenneth H Downing / ![]() |
| PubMed Abstract | We have used cryo-electron microscopy of kinesin-decorated microtubules to resolve the structure of the motor protein kinesin's crucial nucleotide response elements, switch I and the switch II helix, ...We have used cryo-electron microscopy of kinesin-decorated microtubules to resolve the structure of the motor protein kinesin's crucial nucleotide response elements, switch I and the switch II helix, in kinesin's poorly understood nucleotide-free state. Both of the switch elements undergo conformational change relative to the microtubule-free state. The changes in switch I suggest a role for it in "ejecting" adenosine diphosphate when kinesin initially binds to the microtubule. The switch II helix has an N-terminal extension, apparently stabilized by conserved microtubule contacts, implying a microtubule activation mechanism that could convey the state of the bound nucleotide to kinesin's putative force-delivering element (the "neck linker"). In deriving this structure, we have adapted an image-processing technique, single-particle reconstruction, for analyzing decorated microtubules. The resulting reconstruction visualizes the asymmetric seam present in native, 13-protofilament microtubules, and this method will provide an avenue to higher-resolution characterization of a variety of microtubule- binding proteins, as well as the microtubule itself. |
External links | J Cell Biol / PubMed:17470637 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 9.0 Å |
| Structure data | |
| Chemicals | ![]() ChemComp-MG: ![]() ChemComp-ADP: ![]() ChemComp-ZN: ![]() ChemComp-GTP: ![]() ChemComp-GDP: ![]() ChemComp-TA1: |
| Source |
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Keywords | TRANSPORT PROTEIN / Motor protein / ATPase |
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