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Literature summary for 7.5.2.B8 extracted from

  • Pretz, M.G.; Albers, S.V.; Schuurman-Wolters, G.; Tampé, R.; Driessen, A.J.; van der Does, C.
    Thermodynamics of the ATPase cycle of GlcV, the nucleotide-binding domain of the glucose ABC transporter of Sulfolobus solfataricus (2006), Biochemistry, 45, 15056-15067.
    View publication on PubMed
Search for more literature for 7.5.2.B8

Cloned(Commentary)

Cloned (Comment) Organism
wild-type nucleotide-binding domains GlcV and the E166A and G144A mutant are expressed in Escherichia coli Saccharolobus solfataricus

Protein Variants

Protein Variants Comment Organism
E166A the wild-type enzyme has a conserved domain structure with two membrane-spanning domains that form the transport channel and two cytosolic nucleotide-binding domains that energize the transport reaction. Binding of ATP to the nucleotide-binding domain monomer results in formation of a nucleotide-binding domain dimer. Hydrolysis of the ATP drives the dissociation of the dimer. The mutant enzymed is defective in dimer dissociation Saccharolobus solfataricus
G144A | the wild-type enzyme has a conserved domain structure with two membrane-spanning domains that form the transport channel and two cytosolic nucleotide-binding domains that energize the transport reaction. Binding of ATP to the nucleotide-binding domain monomer results in formation of a nucleotide-binding domain dimer. Hydrolysis of the ATP drives the dissociation of the dimer. The mutant enzyme is unable to dimerize Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus
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-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Saccharolobus solfataricus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + D-glucose/out
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 Saccharolobus solfataricus ADP + phosphate + D-glucose/in
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 ?

Synonyms

Synonyms Comment Organism
glucose ABC transporter
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 Saccharolobus solfataricus