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Article

Nucleotide-free MalK drives the transition of the maltose transporter to the inward-facing conformation.

The Journal of biological chemistry - 4 Apr 2014

Bao Huan, Duong Franck

Abstract excerpt

The complex MalFGK2 hydrolyzes ATP and alternates between inward- and outward-facing conformations during maltose transport. It has been shown that ATP promotes closure of MalK2 and opening of MalFG toward the periplasm. Yet, why the transporter rests in a conformation facing the cytosol in the absence of nucleotide and how it returns to this state after hydrolysis of ATP is unknown. The membrane domain MalFG may...

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Identifiers

PMID: 24526688
DOI: 10.1074/jbc.M113.545525
PMCID: PMC3975029

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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.

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