Phosphatidylinositol phosphate kinase: a link between protein kinase and glutathione synthase folds.
Comparisons of serine/threonine protein kinase (PK) and type IIbeta phosphatidylinositol phosphate kinase (PIPK) structures with each other and also with other proteins reveal structural and functional similarity between the two kinases and proteins of the glutathione synthase fold (ATP-grasp). This suggests that these enzymes are evolutionarily related. The structure of PIPK, which clearly resembles both PK and ATP-grasp, provides a link between the two proteins and establishes that the C-terminal domains of PK, PIPK and ATP-grasp share the same fold. The functional implications of the proposed homology are discussed.
Grishin
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National Library of Medicine, National Institutes of Health, Bldg. 38A, Bethesda, MD, 20894, USA. grishin@ncbi.nlm.nih.gov
D000595:Amino Acid Sequence; D005981:Glutathione Synthase / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017853:Phosphotransferases (Alcohol Group Acceptor) / Q000737:chemistry*; D017510:Protein Folding; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry*; D017433:Protein Structure, Secondary
D017853:Phosphotransferases (Alcohol Group Acceptor); C020077:1-phosphatidylinositol-4-phosphate 5-kinase; D017346:Protein Serine-Threonine Kinases; D005981:Glutathione Synthase