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Literature summary for 3.4.21.105 extracted from

  • Ha, Y.
    Structure and mechanism of intramembrane protease (2009), Semin. Cell Dev. Biol., 20, 240-250.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of Escherichia coli GlpG consists of a 6-transmembrane domain topology Toxoplasma gondii
structure of Escherichia coli GlpG consists of a 6-transmembrane domain topology Escherichia coli
structure of Escherichia coli GlpG consists of a 6-transmembrane domain topology. The active site of Escherichia coli GlpG is found at the bottom of a shallow pocket that faces the extracellular side of the membrane. Above the catalytic dyad is a loop structure which lies roughly parallel to the membrane plane. A side chain from the loop (Phe-245) drops down and seals a gap between two transmembrane helices. This loop structure sterically hinders substrate access to the catalytic serine and is intrinsically flexible Plasmodium falciparum

Protein Variants

Protein Variants Comment Organism
H2541X using mutagenesis it is shown that His254 is catalytically essential Plasmodium falciparum
H2541X using mutagenesis it is shown that His254 is catalytically essential Toxoplasma gondii
H2541X using mutagenesis it is shown that His254 is catalytically essential Escherichia coli
S201X using mutagenesis it is shown that Ser201 is catalytically essential Plasmodium falciparum
S201X using mutagenesis it is shown that Ser201 is catalytically essential Toxoplasma gondii
S201X using mutagenesis it is shown that Ser201 is catalytically essential Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
3,4-dichloroisocoumarin
-
Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Drosophila melanogaster 16020
-
mitochondrion
-
Saccharomyces cerevisiae 5739
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
growth-factor gurken + H2O Drosophila melanogaster
-
?
-
?
growth-factor spitz + H2O Drosophila melanogaster
-
?
-
?

Organism

Organism UniProt Comment Textmining
Drosophila melanogaster
-
-
-
Escherichia coli P09391
-
-
Plasmodium falciparum
-
-
-
Saccharomyces cerevisiae
-
-
-
Toxoplasma gondii
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
adhesin EBP-175 + H2O adhesin EBP-175 of Plasmodium falciparum undergoes ectodomain shedding, in a reaction catalyzed by plasmodium rhomboid pfROM4. pfROM4 cleaves within the transmembrane region of the adhesin Plasmodium falciparum ?
-
?
adhesin MIC2 + H2O the ectodomain of Toxoplasma gondii adhesin MIC2, a type-I membrane protein is cleaved by rhomboid Toxoplasma gondii ?
-
?
Ccp1 + H2O Ccp1 is a mitochondrial cytochrome c peroxidase its cleavage side resides in a short stretch of moderately hydrophobic sequence Saccharomyces cerevisiae ?
-
?
growth-factor gurken + H2O
-
Drosophila melanogaster ?
-
?
growth-factor spitz + H2O
-
Drosophila melanogaster ?
-
?
Mgm1 + H2O Mgm1 is a dynamin-like GTPase its cleavage side resides in a short stretch of moderately hydrophobic sequence Saccharomyces cerevisiae ?
-
?
additional information an artificial fusion protein bearing the sequence around the second transmembrane domain of LacY is cleavable by Escherichia coli GlpG in intact bacterial cells (LacY itself is not a substrate for rhomboid). A Ser-Asp bond is cleaved Escherichia coli ?
-
?

Synonyms

Synonyms Comment Organism
GlpG
-
Escherichia coli
pfROM4
-
Plasmodium falciparum
Rhomboid
-
Drosophila melanogaster
rhomboid Pcp1/Rbd1
-
Saccharomyces cerevisiae
TgROM5
-
Toxoplasma gondii

General Information

General Information Comment Organism
malfunction rhomboid is required for pattern formation in the ventral ectoderm, in which mutation causes a rhomboid-shaped head skeleton. This phenotype is due to the role of fly rhomboid in epidermal growth factor receptor signaling Drosophila melanogaster