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Literature summary for 7.6.2.9 extracted from

  • Gul, N.; Schuurman-Wolters, G.; Karasawa, A.; Poolman, B.
    Functional characterization of amphipathic alpha-helix in the osmoregulatory ABC transporter OpuA (2012), Biochemistry, 51, 5142-5152.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Lactococcus lactis Lactococcus lactis

Protein Variants

Protein Variants Comment Organism
additional information deletion of the amphipathic alpha-helix inactivates OpuA. Deleting part of the helix but leaving the amino-terminus and linker region intact results in a major decrease in activity. The amphipathic alpha-helix is critical for maximal activity but not for the ionic regulation of the transporter Lactococcus lactis
S24C mutations in the amphipathic alpha-helix fused to the core of the transmembrane domain of the OpuABC subunit. Mutation does not have distant structural effects on the overall conformation of the transporter Lactococcus lactis
T23C mutations in the amphipathic alpha-helix fused to the core of the transmembrane domain of the OpuABC subunit. Mutation does not have distant structural effects on the overall conformation of the transporter Lactococcus lactis
T25C mutations in the amphipathic alpha-helix fused to the core of the transmembrane domain of the OpuABC subunit. Mutation does not have distant structural effects on the overall conformation of the transporter Lactococcus lactis

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane the amphipathic alpha-helix fused to the core of the transmembrane domain of the OpuABC subunit is located close to the membrane surface, where its hydrophobic face interacts with the transport protein rather than the membrane lipids. The amphipathic alpha-helix of OpuA is necessary for high activity of OpuA but is not critical for the biogenesis of the protein or the ionic regulation of transport Lactococcus lactis 16020
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Organism

Organism UniProt Comment Textmining
Lactococcus lactis
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-
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Synonyms

Synonyms Comment Organism
OpuA
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Lactococcus lactis

General Information

General Information Comment Organism
physiological function the amphipathic alpha-helix fused to the core of the transmembrane domain of the OpuABC subunit is located close to the membrane surface, where its hydrophobic face interacts with the transport protein rather than the membrane lipids. The amphipathic alpha-helix of OpuA is necessary for high activity of OpuA but is not critical for the biogenesis of the protein or the ionic regulation of transport Lactococcus lactis