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Article

Evidence for multiple pathways in the assembly of the Escherichia coli maltose transport complex.

The Journal of biological chemistry - 6 Aug 2004

Kennedy Kathleen A, Gachelet Eliora G, Traxler Beth

Abstract excerpt

We used the maltose transport complex MalFGK2 of the Escherichia coli cytoplasmic membrane as a model for the study of the assembly of hetero-oligomeric membrane protein complexes. Analysis of other membrane protein complexes has led to a general model in which a unique, ordered pathway is followed from subunit monomers to a final oligomeric structure. In contrast, the studies reported here point to a...

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Identifiers

PMID: 15192116
DOI: 10.1074/jbc.M403796200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Evidence for multiple pathways in the assembly of the Escherichia coli maltose transport complex.PMID 15192116Read ↗

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

The maltose ABC transporter: action of membrane lipids on the transporter stability, coupling and ATPase activity.Semantic proximity Read ↗

Discovery of an auto-regulation mechanism for the maltose ABC transporter MalFGK2.Semantic proximity Read ↗

Nucleotide-free MalK drives the transition of the maltose transporter to the inward-facing conformation.Semantic proximity Read ↗

Protein complexes of the Escherichia coli cell envelope.Semantic proximity Read ↗

Overproduction, solubilization, and reconstitution of the maltose transport system from Escherichia coli.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 ↗

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

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

Crystal structure of a catalytic intermediate of the maltose transporter.Semantic proximity Read ↗

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