A model for the catalytic site of F1-ATPase based on analogies to nucleotide-binding domains of known structure.
An updated topological model is constructed for the catalytic nucleotide-binding site of the F1-ATPase. The model is based on analogies to the known structures of the MgATP site on adenylate kinase and the guanine nucleotide sites on elongation factor Tu (Ef-Tu) and the ras p21 protein. Recent studies of these known nucleotide-binding domains have revealed several common functional features and similar alignment of nucleotide in their binding folds, and these are used as a framework for evaluating results of affinity labeling and mutagenesis studies of the beta subunit of F1. Several potentially important residues on beta are noted that have not yet been studied by mutagenesis or affinity labeling.
Duncan
T M
TM
Department of Biochemistry and Molecular Biology, SUNY Health Science Center, Syracuse 13210.
Cross
R L
RL
D000263:Adenylate Kinase / Q000737:chemistry; D000595:Amino Acid Sequence; D001665:Binding Sites; D002384:Catalysis; D004926:Escherichia coli; D008956:Models, Chemical; D008969:Molecular Sequence Data; D009711:Nucleotides / Q000378:metabolism; D010444:Peptide Elongation Factor Tu / Q000737:chemistry; D016283:Proto-Oncogene Proteins p21(ras) / Q000737:chemistry; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000378:metabolism
D009711:Nucleotides; D000263:Adenylate Kinase; D010444:Peptide Elongation Factor Tu; D006180:Proton-Translocating ATPases; D016283:Proto-Oncogene Proteins p21(ras)