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Literature summary for 5.3.99.3 extracted from

  • Sjoegren, T.; Nord, J.; Ek, M.; Johansson, P.; Liu, G.; Geschwindner, S.
    Crystal structure of microsomal prostaglandin E2 synthase provides insight into diversity in the MAPEG superfamily (2013), Proc. Natl. Acad. Sci. USA, 110, 3806-3811.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
isozyme mPGES-1, recombinant functional expression in Spodoptera frugiperda Sf9 cells using the baculovirus transfection method Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant microsomal isozyme PGE2 synthase-1, in presence of beta-octyl-glycoside and GSH or 1-(4-phenylphenyl)-2-(S-glutathionyl)-ethanone (bis-phenyl-GSH), hanging drop vapor diffusion method, the reservoir solutions used contain 100 mM CAPSO, pH 9.5, 30% PEG 400, 100 mM NaCl, and 100 mM Li2SO4 (mersalyl acid soak and bis-phenyl-GSH complex) or 100 mM Tris, pH 8.0-8.5, 30% PEG400, 100 mM NaCl, and 1 mM TCEP (native GSH complex), 4°C, X-ray diffraction structure determination and analysis at 1.2 A resolution Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
microsome microsomal isozyme PGE2 synthase-1 Homo sapiens
-
-

Organism

Organism UniProt Comment Textmining
Homo sapiens O14684 isozyme microsomal PGE2 synthase-1
-

Purification (Commentary)

Purification (Comment) Organism
recombinant active isozyme mPGES-1 from Spodoptera frugiperda Sf9 cell microsomes by hydroxylapatite chromatography Homo sapiens

Synonyms

Synonyms Comment Organism
microsomal PGE2 synthase-1
-
Homo sapiens
mPGES-1
-
Homo sapiens

General Information

General Information Comment Organism
evolution microsomal prostaglandin E2 synthase belongs to the MAPEG superfamily Homo sapiens
additional information the isozyme mPGES-1 structure reveals three well-defined active site cavities within the membrane-spanning region in each monomer interface of the trimeric structure. An important determinant of the active site cavity is a small cytosolic domain inserted between transmembrane helices I and II. A a 16-A-deep cone-shaped cavity extending from the cytosolic side into the membrane-spanning region might have a potential role in substrate access. Serine 127 plays a role in the catalytic mechanism, active site structure, overview Homo sapiens