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Nature. 1992 Aug 27;358(6389):727-33.

Crystal structures explain functional properties of two E. coli porins.

Author information

1
Department of Structural Biology, University of Basel, Switzerland.

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 beta-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.

PMID:
1380671
DOI:
10.1038/358727a0
[Indexed for MEDLINE]

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