Journal article
Crystal structures explain functional properties of two E. coli porins.
- Cowan SW Department of Structural Biology, University of Basel, Switzerland.
- Schirmer T
- Rummel G
- Steiert M
- Ghosh R
- Pauptit RA
- Jansonius JN
- Rosenbusch JP
- 1992-08-27
Published in:
- Nature. - 1992
Amino Acid Sequence
Bacterial Outer Membrane Proteins
Computer Graphics
Crystallography
Escherichia coli
Ion Channels
Models, Molecular
Molecular Sequence Data
Mutation
Porins
Protein Conformation
Solubility
Structure-Activity Relationship
Water
X-Ray Diffraction
English
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.
- Language
-
- English
- Open access status
- closed
- Identifiers
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- DOI 10.1038/358727a0
- PMID 1380671
- Persistent URL
- https://sonar.ch/global/documents/233018
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