2bon

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{{STRUCTURE_2bon| PDB=2bon | SCENE= }}
{{STRUCTURE_2bon| PDB=2bon | SCENE= }}
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'''STRUCTURE OF AN ESCHERICHIA COLI LIPID KINASE (YEGS)'''
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===STRUCTURE OF AN ESCHERICHIA COLI LIPID KINASE (YEGS)===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_17351295}}
==About this Structure==
==About this Structure==
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[[Category: Lipid kinase,dag kinase,atp-binding]]
[[Category: Lipid kinase,dag kinase,atp-binding]]
[[Category: Transferase]]
[[Category: Transferase]]
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Revision as of 00:39, 28 July 2008

Image:2bon.png

Template:STRUCTURE 2bon

STRUCTURE OF AN ESCHERICHIA COLI LIPID KINASE (YEGS)

Template:ABSTRACT PUBMED 17351295

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

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