2bon
From Proteopedia
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'''STRUCTURE OF AN ESCHERICHIA COLI LIPID KINASE (YEGS)''' | '''STRUCTURE OF AN ESCHERICHIA COLI LIPID KINASE (YEGS)''' | ||
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[[Category: Johnson, K A.]] | [[Category: Johnson, K A.]] | ||
[[Category: Nordlund, P.]] | [[Category: Nordlund, P.]] | ||
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Revision as of 17:34, 3 May 2008
STRUCTURE OF AN ESCHERICHIA COLI LIPID KINASE (YEGS)
Overview
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.
About this Structure
2BON is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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 Jul 6;282(27):19644-52. Epub 2007 Mar 11. PMID:17351295 Page seeded by OCA on Sat May 3 20:34:55 2008
