2JGR

Crystal structure of YegS in complex with ADP

Summary for 2JGR

• Entry DOI: 10.2210/pdb2jgr/pdb
• Related: 2BON
• Descriptor: YEGS, PYROPHOSPHATE 2- (3 entities in total)
• Functional Keywords: phosphatidylglycerole kinase, transferase, lipid kinase, pyrrophosphate, hypothetical protein
• Biological source: ESCHERICHIA COLI
• Cellular location: Cytoplasm: P76407
• Total number of polymer chains: 1
• Total formula weight: 32570.75

Authors

Bakali, H.M.,Herman, M.D.,Johnson, K.A.,Kelly, A.A.,Wieslander, A.,Hallberg, B.M.,Nordlund, P. (deposition date: 2007-02-14, release date: 2007-05-15, Last modification date: 2024-10-23)

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

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: 17351295
DOI: 10.1074/JBC.M604852200

Experimental method

X-RAY DIFFRACTION (2.65 Å)