Eg5 is a homotetrameric kinesin-5 motor protein that generates outward force on the
overlapping, antiparallel microtubules (MTs) of the mitotic spindle. Upon binding an MT, an
Eg5 dimer releases one ADP molecule, undergoes a slow (∼ 0.5 s− 1) isomerization, and
finally releases a second ADP, adopting a tightly MT-bound, nucleotide-free (APO)
conformation. This conformation precedes ATP binding and stepping. Here, we use
mutagenesis, steady-state and pre-steady-state kinetics, motility assays, and electron …

Eg5 is a homotetrameric kinesin-5 motor protein that generates outward force on the
overlapping, antiparallel microtubules (MTs) of the mitotic spindle. Upon binding a MT, an
Eg5 dimer releases one ADP molecule, undergoes a slow (∼ 0.5 s-1) isomerization, and
finally releases a second ADP, adopting a tightly MT-bound, nucleotide-free (APO)
conformation. This conformation precedes ATP binding and stepping. Here, we use
mutagenesis, steady-state and presteady-state kinetics, motility assays, and electron …