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2P4N

Human Monomeric Kinesin (1BG2) and Bovine Tubulin (1JFF) Docked into the 9-Angstrom Cryo-EM Map of Nucleotide-Free Kinesin Complexed to the Microtubule

Summary for 2P4N
Entry DOI10.2210/pdb2p4n/pdb
Related1BG2 1JFF
EMDB information1340
DescriptorKinesin heavy chain, Tubulin alpha chain, Tubulin beta chain, ... (9 entities in total)
Functional Keywordsmotor protein, atpase, transport protein
Biological sourceHomo sapiens (human)
More
Total number of polymer chains3
Total formula weight138795.61
Authors
Sindelar, C.V.,Downing, K.H. (deposition date: 2007-03-12, release date: 2008-07-08, Last modification date: 2024-02-21)
Primary citationSindelar, C.V.,Downing, K.H.
The beginning of kinesin's force-generating cycle visualized at 9-A resolution.
J.Cell Biol., 177:377-385, 2007
Cited by
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, 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.
PubMed: 17470637
DOI: 10.1083/jcb.200612090
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (9 Å)
Structure validation

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