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 DOI | 10.2210/pdb2p4n/pdb |
Related | 1BG2 1JFF |
EMDB information | 1340 |
Descriptor | Kinesin heavy chain, Tubulin alpha chain, Tubulin beta chain, ... (9 entities in total) |
Functional Keywords | motor protein, atpase, transport protein |
Biological source | Homo sapiens (human) More |
Total number of polymer chains | 3 |
Total formula weight | 138795.61 |
Authors | Sindelar, C.V.,Downing, K.H. (deposition date: 2007-03-12, release date: 2008-07-08, Last modification date: 2024-02-21) |
Primary citation | Sindelar, 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: 17470637DOI: 10.1083/jcb.200612090 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (9 Å) |
Structure validation
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