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Literature summary extracted from

  • Oldham, M.; Chen, J.
    Crystal structure of the maltose transporter in a pretranslocation intermediate state (2011), Science, 332, 1202-1205.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
7.5.2.1 maltose-binding protein a periplasmic maltose-binding protein, MBP, is required to stimulate the ATPase activity of the transporter. MBP stimulates ATP hydrolysis and initiates the transport process, it must interact with the resting state conformation to form a pretranslocation complex that is metastable in order to advance to the outward-facing conformation in the presence of ATP Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
7.5.2.1 pre-translocation, outward- and inward-facing crystal structure analysis of enzyme complex with or without bound maltose binding protein and bound maltose and ATP, overview Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.5.2.1 membrane transmembrane protein complex Escherichia coli 16020
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7.5.2.1 ATP + H2O + maltose/out Escherichia coli
-
 ADP + phosphate + maltose/in
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
7.5.2.1 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.5.2.1 ATP + H2O + maltose/out
-
 Escherichia coli ADP + phosphate + maltose/in
-
 ?
7.5.2.1 ATP + H2O + maltose/out structure and transport mechanism, overview Escherichia coli ADP + phosphate + maltose/in
-
 ?

Subunits

EC Number Subunits Comment Organism
7.5.2.1 More the maltose transporter is an importer composed of two transmembrane subunits, MalF and MalG, and two subunits of a cytoplasmic adenosine triphosphatase (ATPase), MalK Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
7.5.2.1 maltose transporter
-
 Escherichia coli

General Information

EC Number General Information Comment Organism
7.5.2.1 additional information in the absence of MBP, MalFGK2 forms an inwardfacing conformation with the transmembrane-maltose-binding site exposed to the cytoplasm Escherichia coli
7.5.2.1 physiological function the maltose ABC transporter MalFGK2 converts chemical energy from ATP hydrolysis to mechanical work for maltose substrate translocation. A periplasmic maltose-binding protein, MBP, is required to stimulate the ATPase activity of the transporter Escherichia coli