2y5w | pdb_00002y5w

CRYSTAL STRUCTURE OF DROSOPHILA MELANOGASTER KINESIN-1 MOTOR DOMAIN DIMER

spinqualitylabelsall models 2y5w, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2y5w is a 2 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ADP, MG Related: 2y65 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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. The structure of the kinesin-1 motor-tail complex reveals the mechanism of autoinhibition.,Kaan HY, Hackney DD, Kozielski F Science. 2011 Aug 12;333(6044):883-5. PMID:21836017 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Kinesin

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