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

In order to search for a common structural motif in the phosphate-bindingsites of protein–mononucleotide complexes, we investigatedthe structural variety of phosphate-binding schemes by an all-against-allcomparison of 491 binding sites found in the Protein Data Bank.We found four frequently occurring structural motifs composedof protein atoms interacting with phosphate groups, each ofwhich appears in different protein superfamilies with differentfolds. The most frequently occurring motif, which we call thestructural P-loop, is shared by 13 superfamilies and is characterizedby a four-residue fragment, GXXX, interacting with a phosphategroup through the backbone atoms. Various sequence motifs, includingWalker's A motif or the P-loop, turn out to be a structuralP-loop found in a few specific superfamilies. The other threemotifs are found in pairs of superfamilies: protein kinase andglutathione synthetase ATPase domain like, actin-like ATPasedomain and nucleotidyltransferase, and FMN-linked oxidoreductaseand PRTase.