MKLP2 is a divergent molecular motor that has structurally evolved to bind its microtubule track and use the energy of ATP in distinct ways, tuned according to its function in cell division.
The motor protein kinesin utilizes its fuel molecule by active and concerted motions of its subdomains, while it rapidly interacts with the microtubule track by forming a wet and dynamic interface.
Probing the DNA motor SpoIIIE at the single-molecule level has revealed its force-generating step, rich translocation dynamics during motor operation and a novel, bi-phasic mechanical response to opposing force.
The protofilaments that curl outward from a disassembling microtubule tip carry a large amount of strain energy and they can drive movement with an efficiency similar to conventional motor proteins.
Precise hydrogen-bond stabilization of the neck linker docking onto the catalytic motor domain, is crucial for motor activity and intracellular functions of the bi-directional mitotic kinesin-5 Cin8.
Individual nonmuscle myosin 2 filaments in cells may differ their mechanical and kinetic properties depending on the myosin paralog composition giving the cells a mechanism for fine tuning the output of a given nonmuscle myosin filament.
The outer domain of the kinetochore can rotate (swivel) around the centromere, and this rather than intra-kinetochore stretching is coupled to anaphase onset.
Cardiac myosin converts energy from ATP into mechanical work by transitioning from a short-lived force-bearing state, to a post working stroke state before the release of inorganic phosphate.
A new optical tweezers assay sheds light on the mechanism of cooperation and force generation by the subunits of RecBCD, critical for the repair of double strand breaks in bacteria.
