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

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1998
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Forst, Doris
Wacker, Thomas
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Nature Structural Biology ; 5 (1998), 1. - pp. 37-46. - ISSN 1072-8368
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 beta-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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ISO 690FORST, Doris, Wolfram WELTE, Thomas WACKER, Kay DIEDERICHS, 1998. Structure of the sucrose-specific porin ScrY from Salmonella typhimurium and its complex with sucrose. In: Nature Structural Biology. 5(1), pp. 37-46. ISSN 1072-8368. Available under: doi: 10.1038/nsb0198-37
BibTex
@article{Forst1998Struc-21081,
  year={1998},
  doi={10.1038/nsb0198-37},
  title={Structure of the sucrose-specific porin ScrY from Salmonella typhimurium and its complex with sucrose},
  number={1},
  volume={5},
  issn={1072-8368},
  journal={Nature Structural Biology},
  pages={37--46},
  author={Forst, Doris and Welte, Wolfram and Wacker, Thomas and Diederichs, Kay}
}
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