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Literature summary for 3.4.21.105 extracted from

  • Ben-Shem, A.; Fass, D.; Bibi, E.
    Structural basis for intramembrane proteolysis by rhomboid serine proteases (2007), Proc. Natl. Acad. Sci. USA, 104, 462-466.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged GlpG in Escherichia coli strain C43(DE3) Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant His-tagged GlpG, hanging drop vapour diffusion method, 5 mg/ml protein in 20 mM HEPES, pH 7.5, 90 mM NaCl, 10% glycerol, and lauryl dimethylamine oxide, mixed with a reservoir solution containing 30% w/v PEG 400, 200 mM CaCl2, and 100 mM MES, pH 6.5, X-ray diffraction structure determination and analysis at 2.25-2.3 A resolution Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane the enzyme contains 6 transmembrane helices and an N-terminal cytoplasmic part Escherichia coli 16020
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Organism

Organism UniProt Comment Textmining
Escherichia coli P09391 gene glpG
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Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged GlpG from membranes of strain C43(DE3) by nickel affinity chromatography Escherichia coli

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 structure-function relationship, catalytic residues are Ser201 of transmembrane helix 4 and His254 of transmembrane helix 6 Escherichia coli

Subunits

Subunits Comment Organism
More structure modeling, structure-function relationship, overview Escherichia coli

Synonyms

Synonyms Comment Organism
GlpG
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Escherichia coli
rhomboid serine protease
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Escherichia coli