   5.6.1.2 | ATP + H2O + a dynein associated with a microtubule at position n = ADP + phosphate + a dynein associated with a microtubule at position n-1 (toward the minus end) |
the active sites for microtubule binding and ATP hydrolysis communicate via conformational changes transduced through a ca. 10 nm length antiparallel coilded-coil stalk, which connects the binding domain to the roughly 300 kDa motor core. A balancing of opposing conformations in the stalk and microtubule binding domain (MTBD) enables modest ling-range interactions arising from ATP-binding in the motor core to induce a reaxation of the MTBD into the stable low affinity state |
712426 |
