title: Mechanical transduction mechanisms of RecA-like molecular motors.
abstract: A majority of ATP-dependent molecular motors are RecA-like proteins, performing diverse functions in biology. These RecA-like molecular motors consist of a highly conserved core containing the ATP-binding site. Here I examined how ATP binding within this core is coupled to the conformational changes of different RecA-like molecular motors. Conserved hydrogen bond networks and conformational changes revealed two major mechanical transduction mechanisms: (1) intra-domain conformational changes and (2) inter-domain conformational changes. The intra-domain mechanism has a significant hydrogen bond rearrangement within the domain containing the P-loop, causing relative motion between two parts of the protein. The inter-domain mechanism exhibits little conformational change in the P-loop domain. Instead, the major conformational change is observed between the P-loop domain and an adjacent domain or subunit containing the arginine finger. These differences in the mechanical transduction mechanisms may link to the underlying energy surface governing a Brownian ratchet or a power stroke.
authors: Department of Mechanical Engineering, Columbia University, New York, NY 10027, USA. jcliao@columbia.edu
authors: Jung-Chi
authors: JC
authors: Liao
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D001665:Binding Sites; D004734:Energy Metabolism; D006860:Hydrogen Bonding; D008958:Models, Molecular; D020409:Molecular Motor Proteins / Q000737:chemistry* / Q000378:metabolism; D009068:Movement; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011938:Rec A Recombinases / Q000737:chemistry* / Q000378:metabolism
chemical_list: D020409:Molecular Motor Proteins; D000255:Adenosine Triphosphate; D011938:Rec A Recombinases