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Literature summary for 3.4.21.105 extracted from

  • Wang, Y.; Zhang, Y.; Ha, Y.
    Crystal structure of a rhomboid family intramembrane protease (2006), Nature, 444, 179-180.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
purified GlpG core domain, hanging drop vapour diffusion method, room temperature, 5 mg/ml membrane protein in 10 mM Tris-HCl, pH 7.6, and 20 mM nonylglucoside, over a reservoir solution of 3 M NaCl and 100 mM Bis-Tris propane, pH 7.0, cryoprotection by 25% glycerol, 1 month, X-ray diffraction structure determination and analysis at 2.1 A resolution Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane integral membrane protein with six transmembrane segments, membrane topology of a rhomboid protease and its substrate, overview Escherichia coli 16020
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Organism

Organism UniProt Comment Textmining
Escherichia coli P09391 gene glpG
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Reaction

Reaction Comment Organism Reaction ID
cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains the active site structure, with a Ser 201 and His 254 catalytic dyad, is accessible by substrate through a large V-shaped opening that faces laterally towards the lipid, but is blocked by a half-submerged loop structure, catalytically involved residues and water molecules, catalytic mechanism, overview Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme cleave the transmembrane domain of other membrane proteins, membrane topology of a rhomboid protease and its substrate, overview Escherichia coli ?
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?
protein MIC2 + H2O cleavage at an Ala-Gly bond Escherichia coli ?
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?

Synonyms

Synonyms Comment Organism
GlpG
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Escherichia coli
More the enzyme belongs to the rhomboid intramembrane protease family Escherichia coli