Article
Crystal structures explain functional properties of two E. coli porins.
Nature - 27 Aug 1992
Cowan S W, Schirmer T, Rummel G, Steiert M, Ghosh R, Pauptit R A, Jansonius J N, Rosenbusch J P
Abstract excerpt
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...
Topics
- Amino Acid Sequence
- Bacterial Outer Membrane Proteins
- Computer Graphics
- Crystallography
- Escherichia coli
- Ion Channels
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Porins
- Protein Conformation