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Crystal structures explain functional properties of two E. coli porins

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Abstract

Porins form aqueous channels that aid the diffusion of small hydrophilic molecules across the outer membrane of Gram-negative bacteria. The crystal structures of matrix porin and phosphoporin both reveal trimers of identical subunits, each subunit consisting of a 16-stranded anti-parallel β-barrel containing a pore. A long loop inside the barrel contributes to a constriction of the channel where the charge distribution affects ion selectivity. The structures explain at the molecular level functional characteristics and their alterations by known mutations.

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Author notes

  1. R. A. Pauptit

    Present address: ICI Pharmaceuticals, Mereside, Alderley Park, Macclesfield, Cheshire, SK10 4TG, UK

Authors and Affiliations

  1. Department of Structural Biology, Biocentre, University of Basel, CH-4056, Basel, Switzerland

    S. W. Cowan, T. Schirmer, G. Rummel, M. Steiert, R. Ghosh, R. A. Pauptit, J. N. Jansonius & J. P. Rosenbusch

  2. Department of Microbiology, Biocentre, University of Basel, CH-4056, Basel, Switzerland

    G. Rummel, M. Steiert, R. Ghosh & J. P. Rosenbusch

Authors
  1. S. W. Cowan
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  2. T. Schirmer
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  3. G. Rummel
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  4. M. Steiert
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  5. R. Ghosh
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  6. R. A. Pauptit
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  7. J. N. Jansonius
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  8. J. P. Rosenbusch
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Cowan, S., Schirmer, T., Rummel, G. et al. Crystal structures explain functional properties of two E. coli porins. Nature 358, 727–733 (1992). https://doi.org/10.1038/358727a0

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  • DOI: https://doi.org/10.1038/358727a0

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