Crystal structure of phosphatidylglycerophosphatase (PGPase), a putative membrane‐bound lipid phosphatase, reveals a novel binuclear metal binding site and two “proton wires”

@article{Kumaran2006CrystalSO,
  title={Crystal structure of phosphatidylglycerophosphatase (PGPase), a putative membrane‐bound lipid phosphatase, reveals a novel binuclear metal binding site and two “proton wires”},
  author={D. Kumaran and J. Bonanno and S. Burley and S. Swaminathan},
  journal={Proteins: Structure},
  year={2006},
  volume={64}
}
Phosphatidylglycerophosphatase (PGPase), an enzyme involved in lipid metabolism, catalyzes formation of phosphatidylglycerol from phosphatidylglycerophosphate. Phosphatidylglycerol is a multifunctional phospholipid, found in the biological membranes of many organisms. Here, we report the crystal structure of Listeria monocytogenes PGPase at 1.8 Å resolution. PGPase, an all‐helical molecule, forms a homotetramer. Each protomer contains an independent active site with two metal ions, Ca2+ and Mg2… Expand
Mitochondrial phosphatase PTPMT1 is essential for cardiolipin biosynthesis.

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