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Literature summary for 7.6.2.10 extracted from

  • Abramson, J.; Kaback, H.R.; Iwata, S.
    Structural comparison of lactose permease and the glycerol-3-phosphate antiporter: members of the major facilitator superfamily (2004), Curr. Opin. Struct. Biol., 14, 413-419.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
X-ray structure, GlpT consists of 12 transmembrane helices, which form a N- and C-terminal domain, the structure reveals a large internal cavity, open toward the cytoplasm but completely closed to the periplasm, the substrate-binding site, formed by two arginine residues, is accessible from only one side of the membrane at a time Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
inner membrane
-
Escherichia coli
-
-

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + glycerol-3-phosphate/out
-
Escherichia coli ADP + phosphate + glycerol-3-phosphate/in
-
?

Synonyms

Synonyms Comment Organism
GlpT
-
Escherichia coli
glycerol-3-phosphate antiporter
-
Escherichia coli