2Y5W
Crystal structure of Drosophila melanogaster kinesin-1 motor domain dimer
Summary for 2Y5W
| Entry DOI | 10.2210/pdb2y5w/pdb |
| Related | 2Y65 |
| Descriptor | KINESIN HEAVY CHAIN, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | motor protein, microtubule associated, atpase |
| Biological source | DROSOPHILA MELANOGASTER (FRUIT FLY) |
| Cellular location | Cytoplasm, cytoskeleton (Probable): P17210 |
| Total number of polymer chains | 2 |
| Total formula weight | 82673.61 |
| Authors | Kaan, H.Y.K.,Hackney, D.D.,Kozielski, F. (deposition date: 2011-01-18, release date: 2011-08-24, Last modification date: 2023-12-20) |
| Primary citation | Kaan, H.Y.K.,Hackney, D.D.,Kozielski, F. The Structure of the Kinesin-1 Motor-Tail Complex Reveals the Mechanism of Autoinhibition. Science, 333:883-, 2011 Cited by PubMed Abstract: When not transporting cargo, kinesin-1 is autoinhibited by binding of a tail region to the motor domains, but the mechanism of inhibition is unclear. We report the crystal structure of a motor domain dimer in complex with its tail domain at 2.2 angstroms and compare it with a structure of the motor domain alone at 2.7 angstroms. These structures indicate that neither an induced conformational change nor steric blocking is the cause of inhibition. Instead, the tail cross-links the motor domains at a second position, in addition to the coiled coil. This "double lockdown," by cross-linking at two positions, prevents the movement of the motor domains that is needed to undock the neck linker and release adenosine diphosphate. This autoinhibition mechanism could extend to some other kinesins. PubMed: 21836017DOI: 10.1126/SCIENCE.1204824 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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