Literature summary for 7.3.2.3 extracted from

Jacobson, B.L.; He, J.J.; Vermersch, P.S.; Lemon, D.D.; Quiocho, F.A.
Engineered interdomain disulfide in the perplasmic receptor for sulfate transport reduces flexibility. Site-directed mutagenesis and ligand-binding studies (1991), J. Biol. Chem., 266, 5220-5225.

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Protein Variants

Protein Variants	Comment	Organism
S129C/G46C	mutation in the periplasmic sulfate receptor, dissociation of sulfate from the mutant enzyme is very slow under oxidizing conditions and increases more than 200-fold when reducing agent is added. This effect is attributed to a loss of interdomain structural flexibility in the presence of the disulfide	Escherichia coli

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
periplasm	sulfate receptor	Escherichia coli	-	-

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
periplasmic sulfate receptor	Escherichia coli

Substrates and Products (Substrate)

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

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Release 2023.1 (January 2023)