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Article

Unliganded maltose-binding protein triggers lactose transport in an Escherichia coli mutant with an alteration in the maltose transport system.

Journal of bacteriology - 1 Dec 1997

Merino G, Shuman H A

Abstract excerpt

Escherichia coli accumulates malto-oligosaccharides by the maltose transport system, which is a member of the ATP-binding-cassette (ABC) superfamily of transport systems. The proteins of this system are LamB in the outer membrane, maltose-binding protein (MBP) in the periplasm, and the proteins of the inner membrane complex (MalFGK2), composed of one MalF, one MalG, and two MalK subunits. Substrate specificity is...

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Identifiers

PMID: 9401026
DOI: 10.1128/jb.179.24.7687-7694.1997
PMCID: PMC179730

Genes

MBP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Unliganded maltose-binding protein triggers lactose transport in an Escherichia coli mutant with an alteration in the maltose transport system.PMID 9401026Read ↗

Truncation of MalF results in lactose transport via the maltose transport system of Escherichia coli.Semantic proximity Read ↗

MalFGK complex assembly and transport and regulatory characteristics of MalK insertion mutants.Semantic proximity Read ↗

Mutation of a single MalK subunit severely impairs maltose transport activity in Escherichia coli.Semantic proximity Read ↗

Mutations that alter the transmembrane signalling pathway in an ATP binding cassette (ABC) transporter.Semantic proximity Read ↗

Novel missense mutations that affect the transport function of MalK, the ATP-binding-cassette subunit of the Salmonella enterica serovar typhimurium maltose transport system.Semantic proximity Read ↗

Uncoupling substrate transport from ATP hydrolysis in the Escherichia coli maltose transporter.Semantic proximity Read ↗

Interaction between maltose-binding protein and the membrane-associated maltose transporter complex in Escherichia coli.Semantic proximity Read ↗

Cellular localization of the MalG protein from the maltose transport system in Escherichia coli K12.Semantic proximity Read ↗

Mechanism of maltose transport in Escherichia coli: transmembrane signaling by periplasmic binding proteins.Semantic proximity Read ↗

Studies of the maltose transport system reveal a mechanism for coupling ATP hydrolysis to substrate translocation without direct recognition of substrate.Semantic proximity Read ↗

Characterization of malT mutants that constitutively activate the maltose regulon of Escherichia coli.Semantic proximity Read ↗

The ATP-binding cassette subunit of the maltose transporter MalK antagonizes MalT, the activator of the Escherichia coli mal regulon.Semantic proximity Read ↗

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