Structure of the nucleotide-binding domain in the beta-subunit of Escherichia coli F1-ATPase.
We propose a working model for the tertiary structure of the nucleotide-binding domain of the beta-subunit of E. coli F1-ATPase, derived from secondary structure prediction and from comparison of the amino acid sequence with the sequences of other nucleotide-binding proteins of known three-dimensional structure. The model is consistent with previously published results of specific chemical modification studies and of analyses of mutations in the beta-subunit and its implications for subunit interactions and catalytic mechanism in F1-ATPases are discussed.
D000595:Amino Acid Sequence; D001665:Binding Sites; D002352:Carrier Proteins; D002373:Cyclic AMP Receptor Protein; D004926:Escherichia coli / Q000201:enzymology*; D008958:Models, Molecular; D011487:Protein Conformation; D006180:Proton-Translocating ATPases
D002352:Carrier Proteins; D002373:Cyclic AMP Receptor Protein; D006180:Proton-Translocating ATPases