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 > Former Organization Units Biozentrum > Structural Biology (Schirmer) |
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UniBasel Contributors: | Schirmer, Tilman |
Item Type: | Article, refereed |
Article Subtype: | Research Article |
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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