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 | 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 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P09391 | gene glpG | - |
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 | 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 | ? | - |
? | |
protein MIC2 + H2O | cleavage at an Ala-Gly bond | Escherichia coli | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
GlpG | - |
Escherichia coli |
More | the enzyme belongs to the rhomboid intramembrane protease family | Escherichia coli |