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Crystal structures explain functional properties of two E. coli porins

Nature volume 358, pages 727–733 (1992)Cite this article

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

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  1. S. W. Cowan
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  2. T. Schirmer
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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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