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

doi:10.1074/jbc.M113.545525

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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...

Topics

ATP-Binding Cassette Transporters
Adenosine Triphosphate
Biological Transport, Active
Catalysis
Cytosol
Escherichia coli
Escherichia coli Proteins
Monosaccharide Transport Proteins
Mutation
Periplasm
Protein Structure, Quaternary
Protein Structure, Tertiary

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Identifiers

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

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