title: Nucleotide-dependent domain motions within rings of the RecA/AAA(+) superfamily.
abstract: The oligomeric rings formed by RecA-fold proteins are mechanochemical motors that perform many important biological functions. Their RecA-fold domains convert the chemical energy of ATP into mechanical work through large nucleotide-dependent conformational changes. This review summarizes recent structural and mechanistic works on the F1-ATPase and HslU regarding to the force generation by individual RecA folds in the context of ring structures. The F1-ATPase ring for example generates the force perpendicular to the ring axis, while the HslU ring generates forces presumably parallel to it. There exists a strong correlation between the directions of forces generated and the orientation of the RecA folds, not only in these two proteins but also in T7 DNA helicase, suggesting that it should be possible to predict the direction of forces generated by other members of this family on the basis of the orientation of their RecA folds.
authors.affiliation: Department of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, New Haven, CT 06520-8114, USA. wang@mail.csb.yale.edu
authors.forename: Jimin
authors.initials: J
authors.lastname: Wang
mesh_terms: D000255:Adenosine Triphosphate / Q000737:chemistry; D019915:DNA Primase / Q000737:chemistry; D008954:Models, Biological; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry; D006180:Proton-Translocating ATPases / Q000737:chemistry; D011938:Rec A Recombinases / Q000737:chemistry*
chemical_list: D011506:Proteins; D000255:Adenosine Triphosphate; D019915:DNA Primase; D011938:Rec A Recombinases; D006180:Proton-Translocating ATPases