A physical model reveals the mechanochemistry responsible for dynein's processive motion.

ABSTRACT: The molecular motor dynein is associated with various cellular activities, such as directed transport along microtubules and the rhythmic beating of the axoneme. Because of the size and complexity of the protein, a detailed understanding of the mechanochemistry that drives dynein's processive motion is lacking. To overcome this deficiency, we developed the first (to our knowledge) computational model for two-headed dynein that couples conformational changes of the motor's subunits to the biochemical steps involved in ATP hydrolysis. Analysis of the model provides what we believe are several novel insights into how the protein functions: 1), structural constraints limit the motion of the free microtubule binding domain to one dimension, increasing the efficiency with which this domain finds

SUBMITTER: Tsygankov D 

PROVIDER: S-EPMC3127196 | biostudies-literature | 2011 Jul

REPOSITORIES: biostudies-literature