Phosphate‐binding sequences in nucleotide‐binding proteins

Abstract

In the three-dimensional model of adenylate kinase, the phosphate-binding site for AMP and ATP has been identified [Pai, E.F. et al. (1977) J. Mol. Biol. 114, 37451. In this region one can distinguish a sequence glycine XXXX glycinelysine. The same sequence is found in many other mononucleotide-binding proteins including elongation factors and oncogenic P2 I proteins. Dinucleotide-binding proteins display a pyrophosphate-binding unit with a glycine pattern different from that of mononucleotide-binding proteins. It has been found that P2l ras protein possesses a strand motif typical for (pyro)phosphate binding of a mononucleotide. A single mutation at position 12 can confer oncogenic activity on the protein. Based on the assumption that amino acid residues which are critical for function are preferentially conserved, we predict from the sequence that glycine residue I5 rather than residue I2 is important for (pyro)phosphate binding.

GAK: a cyclin G associated kinase contains a tensin/auxilin‐like domain1

“…This recognition site is also found in auxilin (KGDLDFTY at position 58-65) but the sequence is less conserved in tensin (SCELDLVY at position 64-71). The kinase domain of GAK harbors two putative nucleotide binding sequences (GXGXXG) at positions 13-18 and 337-342 [23]. One (KKLS at position 90-93), 19 and 24 potential phosphorylation sites for cAMP-dependent protein kinase, protein kinase C and casein kinase II protein kinase, respectively, were also found (locations are not shown).…”

Primary structure of the β‐subunit of Torpedo californica (Na+ + K+)‐ATPase deduced from the cDNA sequence

“…However, they seem not to be sufficiently hydrophobic to form transmembrane segments (fig.4). It is also to be noted that the sequence Gly-X-Gly-X-X-Gly (X can be any amino acid), which is characteristic of the nucleotide binding region of nucleotide binding proteins [38], is found in the P-subunit (residues 233-238). The functional implication of this sequence is not known because no information is available as to the role of the P-subunit in nucleotide binding.…”

Primary structure of elongation factor 1γ from Artemia

“…Judged from the hydrophobicity plot as shown in fig.4 we observed a remarkable alternation of hydrophobic and hydrophilic regions bordering a large hydrophilic region in the middle of the sequence. The EF-17 sequence does not contain a consensus sequence for ATP or GTP binding [21,22].…”