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Literature summary for 7.5.2.1 extracted from

  • Grote, M.; Bordignon, E.; Polyhach, Y.; Jeschke, G.; Steinhoff, H.J.; Schneider, E.
    A comparative electron paramagnetic resonance study of the nucleotide-binding domains catalytic cycle in the assembled maltose ATP-binding cassette importer (2008), Biophys. J., 95, 2924-2938.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 7.5.2.1

Cloned(Commentary)

Cloned (Comment) Organism
recombinant His-tagged enzyme expression in Escherichia coli strain JM109 Salmonella enterica subsp. enterica serovar Typhimurium
recombinant His-tagged enzyme expression in Escherichia coli strain JM109 Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
vanadate
-
 Escherichia coli
vanadate
-
 Salmonella enterica subsp. enterica serovar Typhimurium

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Salmonella enterica subsp. enterica serovar Typhimurium
Mg2+ required Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P68187
-
-
Salmonella enterica subsp. enterica serovar Typhimurium
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain JM109 Salmonella enterica subsp. enterica serovar Typhimurium
recombinant His-tagged enzyme from Escherichia coli strain JM109 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information although MalF and MalG differ in the number of transmembrane segments of 8 and 6, respectively, and their amino acid sequences, both contain the so-called EAA-motif, i.e. L-loop or coupling helix, which is in contact with MalK. MalF and MalG form a large central cavity for transport, but maltose is only bound to MalF. The MalK subunits bind and hydrolyze ATP, thereby generating the power stroke necessary for the rearrangements of MalFG, quantitative analysis of conformational changes of the nucleotide-binding subunits, MalK2, of the maltose ATP-binding cassette importer MalFGK2 during the transport cycle, overview Salmonella enterica subsp. enterica serovar Typhimurium ?
-
 ?
additional information quantitative analysis of conformational changes of the nucleotide-binding subunits, MalK2, of the maltose ATP-binding cassette importer MalFGK2 during the transport cycle, overview Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
More the maltose transporter consists of two transmembrane subunits, MalF and MalG, a homodimer of the nucleotide-binding subunits, MalK2, at the cytoplasmic side of the membrane and the periplasmic maltose-binding protein, MalE Salmonella enterica subsp. enterica serovar Typhimurium
More the maltose transporter consists of two transmembrane subunits, MalF and MalG, a homodimer of the nucleotide-binding subunits, MalK2, at the cytoplasmic side of the membrane and the periplasmic maltose-binding protein, MalE Escherichia coli

Synonyms

Synonyms Comment Organism
maltose ATP-binding cassette importer
-
 Salmonella enterica subsp. enterica serovar Typhimurium
maltose ATP-binding cassette importer
-
 Escherichia coli