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Structure of the sucrose-specific porin ScrY from Salmonella typhimurium and its complex with sucrose

Nature Structural Biology volume 5, pages 37–46 (1998)Cite this article

Abstract

The X-ray structure of a sucrose-specific porin (ScrY) from Salmonella typhimurium has been determined by multiple isomorphous replacement at 2.4 Å resolution both in its uncomplexed form and with bound sucrose. ScrY is a noncrystallographic trimer of identical subunits, each with 413 structurally well-defined amino acids. A monomer is built up of 18 anti-parallel β-strands surrounding a hydrophilic pore, with a topology closely similar to that of maltoporin. Two non-overlapping sucrose-binding sites were identified in difference Fourier maps. The higher permeability for sucrose of ScrY as compared to maltoporin is mainly accounted for by differences in their pore-lining residues.

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  1. Institut für Biophysik und Strahlenbiologie, Albert-Ludwigs-Universität, Albertstr. 23, 79104, Freiburg im Breisgau, Germany

    Doris Forst & Thomas Wacker

  2. Fakultät für Biologie, Universität Konstanz, Box M656, 78457, Konstanz, Germany

    Wolfram Welte & Kay Diederichs

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Forst, D., Welte, W., Wacker, T. et al. Structure of the sucrose-specific porin ScrY from Salmonella typhimurium and its complex with sucrose. Nat Struct Mol Biol 5, 37–46 (1998). https://doi.org/10.1038/nsb0198-37

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