We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2jgr

From Proteopedia

Revision as of 15:41, 20 March 2008 by OCA (Talk | contribs)
Jump to: navigation, search


PDB ID 2jgr

Drag the structure with the mouse to rotate
, resolution 2.65Å
Sites:
Ligands:
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF YEGS IN COMPLEX WITH ADP


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

2JGR 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 Thu Mar 20 17:41:41 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools