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Literature summary extracted from

  • Kumaran, D.; Bonanno, J.B.; Burley, S.K.; Swaminathan, S.
    Crystal structure of phosphatidylglycerophosphatase (PGPase), a putative membrane-bound lipid phosphatase, reveals a novel binuclear metal binding site and two "proton wires" (2006), Proteins, 64, 851-862.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.3.27 expressed in Escherichia coli BL21 (DE3) cells Listeria monocytogenes

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.3.27 with precipitant containing 30% pentaerythritol ethoxylate, 50 mM ammonium sulfate, 50 mM Bis-Tris at pH 6.5 Listeria monocytogenes

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.3.27 Ca2+ each protomer contains an independent active site with two metal ions, Ca2+ and Mg2+, forming a heterobinuclear center located in a hydrophilic cavity near the surface of the molecule Listeria monocytogenes
3.1.3.27 Mg2+ each protomer contains an independent active site with two metal ions, Ca2+ and Mg2+, forming a heterobinuclear center located in a hydrophilic cavity near the surface of the molecule Listeria monocytogenes

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.27 Listeria monocytogenes
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.27 phosphatidylglycerol 3-phosphate + H2O
-
 Listeria monocytogenes phosphatidylglycerol + phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.3.27 homotetramer x-ray crystallography Listeria monocytogenes

Synonyms

EC Number Synonyms Comment Organism
3.1.3.27 PGPase
-
 Listeria monocytogenes