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CRYSTAL-STRUCTURES EXPLAIN FUNCTIONAL-PROPERTIES OF 2 ESCHERICHIA-COLI PORINS
Author(s): COWAN SW, SCHIRMER T, RUMMEL G, STEIERT M, GHOSH R, PAUPTIT RA, JANSONIUS JN, ROSENBUSCH JP
Source: NATURE    Volume: 358    Issue: 6389    Pages: 727-733    Published: AUG 27 1992  
Times Cited: 990     References: 58     
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.
Document Type: Article
Language: English
Addresses:
1. UNIV BASEL, BIOCTR, DEPT STRUCT BIOL, CH-4056 BASEL, SWITZERLAND
2. UNIV BASEL, BIOCTR, DEPT MICROBIOL, CH-4056 BASEL, SWITZERLAND
Publisher: MACMILLAN MAGAZINES LTD, PORTERS SOUTH, 4 CRINAN ST, LONDON, ENGLAND N1 9XW
Subject Category: Multidisciplinary Sciences
IDS Number: JK699
ISSN: 0028-0836
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