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Crystal structures explain functional properties of two E. coli porins

Cowan, S. W. and Schirmer, T. and Rummel, G. and Steiert, M. and Ghosh, R. and Pauptit, R. A. and Jansonius, J. N. and Rosenbusch, J. P.. (1992) Crystal structures explain functional properties of two E. coli porins. Nature, Vol. 358. pp. 727-733.

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Official URL: http://edoc.unibas.ch/dok/A5258291

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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 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.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Schirmer)
UniBasel Contributors:Schirmer, Tilman
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Publisher:Macmillan
ISSN:0028-0836
Note:Publication type according to Uni Basel Research Database: Journal article
Last Modified:22 Mar 2012 14:20
Deposited On:22 Mar 2012 13:20

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