2BON
Structure of an Escherichia coli lipid kinase (YegS)
Summary for 2BON
| Entry DOI | 10.2210/pdb2bon/pdb |
| Descriptor | LIPID KINASE, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | dag kinase, transferase |
| Biological source | ESCHERICHIA COLI (ESCHERICHIA COLI) |
| Cellular location | Cytoplasm: P76407 |
| Total number of polymer chains | 2 |
| Total formula weight | 71910.10 |
| Authors | Bakali, H.M.,Johnson, K.A.,Hallberg, B.M.,Herman, M.D.,Nordlund, P. (deposition date: 2005-04-12, release date: 2006-10-18, Last modification date: 2024-05-08) |
| Primary citation | Bakali, H.M.,Herman, M.D.,Johnson, K.A.,Kelly, A.A.,Wieslander, A.,Hallberg, B.M.,Nordlund, P. Crystal Structure of Yegs, a Homologue to the Mammalian Diacylglycerol Kinases, Reveals a Novel Regulatory Metal Binding Site. J.Biol.Chem., 282:19644-, 2007 Cited by PubMed 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. PubMed: 17351295DOI: 10.1074/JBC.M604852200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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