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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6389
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pubmed:dateCreated |
1992-9-22
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0028-0836
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
27
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pubmed:volume |
358
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pubmed:geneSymbol |
ompF,
phoE
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
727-33
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1380671-Amino Acid Sequence,
pubmed-meshheading:1380671-Bacterial Outer Membrane Proteins,
pubmed-meshheading:1380671-Computer Graphics,
pubmed-meshheading:1380671-Crystallography,
pubmed-meshheading:1380671-Escherichia coli,
pubmed-meshheading:1380671-Ion Channels,
pubmed-meshheading:1380671-Models, Molecular,
pubmed-meshheading:1380671-Molecular Sequence Data,
pubmed-meshheading:1380671-Mutation,
pubmed-meshheading:1380671-Porins,
pubmed-meshheading:1380671-Protein Conformation,
pubmed-meshheading:1380671-Solubility,
pubmed-meshheading:1380671-Structure-Activity Relationship,
pubmed-meshheading:1380671-Water,
pubmed-meshheading:1380671-X-Ray Diffraction
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pubmed:year |
1992
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pubmed:articleTitle |
Crystal structures explain functional properties of two E. coli porins.
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pubmed:affiliation |
Department of Structural Biology, University of Basel, Switzerland.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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