The predicted secondary structures of the nucleotide-binding sites of six cation-transporting ATPases lead to a probable tertiary fold.
Six cation-dependent transporting ATPases have homologous sequences in the region asigned by chemical labelling to nucleotide binding. Comparison of the most highly conserved segments with other nucleotide-binding domains showed that the sequences were consistent with a mononucleotide-binding fold and enabled a number of likely folding topologies to be limited to two or three alternatives. One of these possible folds was topologically equivalent to adenylate kinase; this was taken as a model in which the significance of conserved amino acids was investigated. In this model conserved amino acids were grouped around a postulated ATP-binding cleft, satisfactorily accounting for their degree of conservation.
Taylor
W R
WR
National Institute for Medical Research, Mill Hill, London, England.
Green
N M
NM
D000251:Adenosine Triphosphatases / Q000032:analysis*; D001665:Binding Sites; D008958:Models, Molecular; D009711:Nucleotides / Q000032:analysis*; D011487:Protein Conformation
D009711:Nucleotides; D000251:Adenosine Triphosphatases