title: Structural mechanism of the ATP-induced dissociation of rigor myosin from actin.
abstract: Myosin is a true nanomachine, which produces mechanical force from ATP hydrolysis by cyclically interacting with actin filaments in a four-step cycle. The principle underlying each step is that structural changes in separate regions of the protein must be mechanically coupled. The step in which myosin dissociates from tightly bound actin (the rigor state) is triggered by the 30 Å distant binding of ATP. Large conformational differences between the crystal structures make it difficult to perceive the coupling mechanism. Energetically accessible transition pathways computed at atomic detail reveal a simple coupling mechanism for the reciprocal binding of ATP and actin.
authors.affiliation: Computational Biochemistry Group, Interdisciplinary Center for Scientific Computing, University of Heidelberg, D-69115 Heidelberg, Germany.
authors.forename: Sebastian
authors.initials: S
authors.lastname: Kühner
authors.forename: Stefan
authors.initials: S
authors.lastname: Fischer
mesh_terms: D000199:Actins / Q000737:chemistry* / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism*; D000818:Animals; D030161:Avian Proteins / Q000737:chemistry / Q000378:metabolism; D001665:Binding Sites; D002645:Chickens; D008954:Models, Biological; D008958:Models, Molecular; D056004:Molecular Dynamics Simulation; D020409:Molecular Motor Proteins / Q000737:chemistry / Q000378:metabolism; D009218:Myosins / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation; D017434:Protein Structure, Tertiary
chemical_list: D000199:Actins; D030161:Avian Proteins; D020409:Molecular Motor Proteins; D000255:Adenosine Triphosphate; D009218:Myosins