2bon

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|PDB= 2bon |SIZE=350|CAPTION= <scene name='initialview01'>2bon</scene>, resolution 1.90&Aring;
|PDB= 2bon |SIZE=350|CAPTION= <scene name='initialview01'>2bon</scene>, resolution 1.90&Aring;
|SITE= <scene name='pdbsite=MGB:Mg+Binding+Site+For+Chain+B'>MGB</scene>
|SITE= <scene name='pdbsite=MGB:Mg+Binding+Site+For+Chain+B'>MGB</scene>
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene>
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bon FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bon OCA], [http://www.ebi.ac.uk/pdbsum/2bon PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bon RCSB]</span>
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}}
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[[Category: Johnson, K A.]]
[[Category: Johnson, K A.]]
[[Category: Nordlund, P.]]
[[Category: Nordlund, P.]]
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[[Category: MG]]
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[[Category: lipid kinase,dag kinase,atp-binding]]
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[[Category: atp-binding]]
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[[Category: dag kinase]]
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[[Category: lipid kinase]]
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:04:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:09:29 2008''

Revision as of 23:09, 30 March 2008


PDB ID 2bon

Drag the structure with the mouse to rotate
, resolution 1.90Å
Sites:
Ligands:
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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

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