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Article Dans Une Revue Journal of Molecular Biology Année : 2000

Extended Sugar Slide Function for the Periplasmic Coiled Coil Domain of ScrY

Résumé

Several bacterial outer membrane proteins have a periplasmic extension whose structure and function remain elusive. Here, the structure/function relationship of the N-terminal periplasmic domain of the sucrose-specific outer membrane channel ScrY was investigated. Circular dichroism and analytical centrifugation demonstrated that the N-terminal domain formed a parallel, three-stranded coiled coil. When this domain was fused to the maltose-specific channel LamB, permeation of maltooligosaccharides in liposomes increased with increasing sugar chain length whereas wild-type LamB showed the opposite effect. Current fluctuation analysis demonstrated increased off-rates for sugar transport through the fusion protein. Moreover, equilibrium dialysis showed an affinity of sucrose for the isolated N-terminal peptide. Together these results demonstrate a novel function for coiled coil domains, operating as an extended sugar slide.

Dates et versions

hal-03621353 , version 1 (28-03-2022)

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Citer

Fabrice Dumas, Sabine Frank, Ralf Koebnik, Emeline Maillet, Ariel Lustig, et al.. Extended Sugar Slide Function for the Periplasmic Coiled Coil Domain of ScrY. Journal of Molecular Biology, 2000, 300 (4), pp.687-695. ⟨10.1006/jmbi.2000.3897⟩. ⟨hal-03621353⟩
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