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Literature summary for 7.5.2.1 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
Search for more literature for 7.5.2.1

Activating Compound

Activating Compound Comment Organism Structure
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)

Crystallization (Comment) Organism
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

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
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

Synonyms Comment Organism
maltose transporter
-
 Escherichia coli

General Information

General Information Comment Organism
additional information in the absence of MBP, MalFGK2 forms an inwardfacing conformation with the transmembrane-maltose-binding site exposed to the cytoplasm Escherichia coli
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