How kinesin waits for ATP affects the nucleotide and load dependence of the stepping kinetics.

ABSTRACT: Conventional kinesin, responsible for directional transport of cellular vesicles, takes multiple nearly uniform 8.2-nm steps by consuming one ATP molecule per step as it walks toward the plus end of the microtubule (MT). Despite decades of intensive experimental and theoretical studies, there are gaps in the elucidation of key steps in the catalytic cycle of kinesin. How the motor waits for ATP to bind to the leading head is controversial. Two experiments using a similar protocol have arrived at different conclusions. One asserts that kinesin waits for ATP in a state with both the heads bound to the MT, whereas the other shows that ATP binds to the leading head after the trailing head detaches. To discriminate between the 2 scenarios, we developed a minimal model, which analytically predic

SUBMITTER: Takaki R 

PROVIDER: S-EPMC6859354 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature