Structural motif of phosphate-binding site common to various protein superfamilies: all-against-all structural comparison of protein–mononucleotide complexes

• Published in: Protein engineering 1999-01, Vol.12 (1), p.11-14
• Main Authors: Kinoshita, Kengo, Sadanami, Keishi, Kidera, Akinori, Go, Nobuhiro
• Format: Article
• Language: English
• Subjects: Actins - chemistry; Binding Sites; convergent evolution; Databases, Factual; FMN Reductase; Glutathione Synthase - chemistry; Models, Molecular; Models, Statistical; NADH, NADPH Oxidoreductases - chemistry; Nucleotidyltransferases - chemistry; Pentosyltransferases - chemistry; phosphate-binding site; Phosphates - metabolism; Protein Conformation; Protein Kinases - chemistry; Protein Structure, Secondary; Proteins - metabolism; Sequence Homology, Amino Acid; structural motif; three-dimensional structure comparison
• ISSN: 0269-2139; 1741-0126; 1460-213X; 1741-0134
• DOI: 10.1093/protein/12.1.11

In order to search for a common structural motif in the phosphate-binding sites of protein–mononucleotide complexes, we investigated the structural variety of phosphate-binding schemes by an all-against-all comparison of 491 binding sites found in the Protein Data Bank. We found four frequently occurring structural motifs composed of protein atoms interacting with phosphate groups, each of which appears in different protein superfamilies with different folds. The most frequently occurring motif, which we call the structural P-loop, is shared by 13 superfamilies and is characterized by a four-residue fragment, GXXX, interacting with a phosphate group through the backbone atoms. Various sequence motifs, including Walker's A motif or the P-loop, turn out to be a structural P-loop found in a few specific superfamilies. The other three motifs are found in pairs of superfamilies: protein kinase and glutathione synthetase ATPase domain like, actin-like ATPase domain and nucleotidyltransferase, and FMN-linked oxidoreductase and PRTase.