Protein Family Models

This entry represents the C-terminal domain found in the YegS protein [1,2]. It is related to the beta sandwich domain of NAD kinases. The structure of YegS reveals a two-domain protein with the active site crevice found between the two domains. The C-terminal domain contains 13 beta-strands and two alpha-helices. The likely substrate for YegS is phosphatidylglycerol [1]. Paper describing PDB structure 2bon. [1]. 17351295. Crystal structure of YegS, a homologue to the mammalian diacylglycerol kinases, reveals a novel regulatory metal binding site. Bakali HM, Herman MD, Johnson KA, Kelly AA, Wieslander A, Hallberg BM, Nordlund P;. J Biol Chem. 2007;282:19644-19652. Paper describing PDB structure 2p1r. [2]. 17393457. Characterization of Salmonella typhimurium YegS, a putative lipid kinase homologous to eukaryotic sphingosine and diacylglycerol kinases. Nichols CE, Lamb HK, Lockyer M, Charles IG, Pyne S, Hawkins AR, Stammers DK;. Proteins. 2007;68:13-25. Paper describing PDB structure 2qv7. [3]. 18611377. Analysis of the Staphylococcus aureus DgkB structure reveals a common catalytic mechanism for the soluble diacylglycerol kinases. Miller DJ, Jerga A, Rock CO, White SW;. Structure. 2008;16:1036-1046. (from Pfam)

Date:

2024-10-16

Diacylglycerol (DAG) is a second messenger that acts as a protein kinase C activator. The catalytic domain is assumed from the finding of bacterial homologues. YegS is the Escherichia coli protein in this family whose crystal structure reveals an active site in the inter-domain cleft formed by four conserved sequence motifs, revealing a novel metal-binding site. The residues of this site are conserved across the family [5]. [1]. 2156169. Porcine diacylglycerol kinase sequence has zinc finger and E-F hand motifs. Sakane F, Yamada K, Kanoh H, Yokoyama C, Tanabe T;. Nature 1990;344:345-348. [2]. 8626538. Molecular cloning of a novel diacylglycerol kinase isozyme with a pleckstrin homology domain and a C-terminal tail similar to those of the EPH family of protein-tyrosine kinases. Sakane F, Imai S, Kai M, Wada I, Kanoh H;. J Biol Chem 1996;271:8394-8401. [3]. 2175712. Purification, cDNA-cloning and expression of human diacylglycerol kinase. Schaap D, de Widt J, van der Wal J, Vandekerckhove J, van Damme J, Gussow D, Ploegh HL, van Blitterswijk WJ, van der Bend RL;. FEBS Lett 1990;275:151-158. [4]. 2159661. Diacylglycerol kinase: a key modulator of signal transduction?. Kanoh H, Yamada K, Sakane F;. Trends Biochem Sci 1990;15:47-50. [5]. 17351295. Crystal structure of YegS, a homologue to the mammalian diacylglycerol kinases, reveals a novel regulatory metal binding site. Bakali HM, Herman MD, Johnson KA, Kelly AA, Wieslander A, Hallberg BM, Nordlund P;. J Biol Chem. 2007;282:19644-19652. (from Pfam)

Date:

2024-10-16

diacylglycerol kinase family lipid kinase such as diacylglycerol (DAG) kinase, which catalyzes the phosphorylation of DAG into phosphatidic acid and is involved in the production of lipoteichoic acid

Date:

2018-01-05

Date:

2021-09-20

Date:

2021-03-12

The E. coli member of this family, YegS has been purified [1] and shown to have phosphatidylglycerol kinase activity. The member from M. tuberculosis, Rv2252, has diacylglycerol kinase activity. BmrU from B. subtilis is in an operon with multidrug efflux transporter Bmr, but is uncharacterized.

Date:

2024-08-07