PMID:17351295

Citation	Bakali, HM, Herman, MD, Johnson, KA, Kelly, AA, Wieslander, A, Hallberg, BM and Nordlund, P (2007) Crystal structure of YegS, a homologue to the mammalian diacylglycerol kinases, reveals a novel regulatory metal binding site. J. Biol. Chem. 282:19644-52
Abstract	The human lipid kinase family controls cell proliferation, differentiation, and tumorigenesis and includes diacylglycerol kinases, sphingosine kinases, and ceramide kinases. YegS is an Escherichia coli protein with significant sequence homology to the catalytic domain of the human lipid kinases. We have solved the crystal structure of YegS and shown that it is a lipid kinase with phosphatidylglycerol kinase activity. The crystal structure reveals a two-domain protein with significant structural similarity to a family of NAD kinases. The active site is located in the interdomain cleft formed by four conserved sequence motifs. Surprisingly, the structure reveals a novel metal binding site composed of residues conserved in most lipid kinases.
Links	PubMed Online version:10.1074/jbc.M604852200
Keywords	Amino Acid Sequence; Animals; Binding Sites; Catalytic Domain; Cell Differentiation/physiology; Cell Proliferation; Crystallography, X-Ray; Diacylglycerol Kinase/chemistry; Escherichia coli/enzymology; Escherichia coli Proteins/chemistry; Humans; Molecular Sequence Data; Phosphotransferases (Alcohol Group Acceptor)/chemistry; Protein Structure, Tertiary; Structural Homology, Protein
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