title: ATP synthase: structure-function relationships.
abstract: Recent work has focused on obtaining a better understanding of the three-dimensional structural relationships between the alpha and beta subunits of the F1 moiety and the location of nucleotide binding domains within these subunits. Four types of approach are currently being pursued: X-ray crystallographic, chemical, molecular biological and biochemical. Here we briefly review some of the major conclusions of these studies, and point out some of the problems that must be resolved before an adequate model that relates structure to function in the ATP synthase molecule can be formulated.
authors.affiliation: Department of Biological Chemistry, Johns Hopkins University, School of Medicine, Baltimore, MD.
authors.forename: P J
authors.initials: PJ
authors.lastname: Thomas
authors.forename: M
authors.initials: M
authors.lastname: Bianchet
authors.forename: D N
authors.initials: DN
authors.lastname: Garboczi
authors.forename: J
authors.initials: J
authors.lastname: Hullihen
authors.forename: L M
authors.initials: LM
authors.lastname: Amzel
authors.forename: P L
authors.initials: PL
authors.lastname: Pedersen
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D008969:Molecular Sequence Data; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000378:metabolism; D013329:Structure-Activity Relationship
chemical_list: D006180:Proton-Translocating ATPases