Porin: Difference between revisions

One representative porin structure is the crystal structure osmoporin OmpC from ''Escherichia coli'' ([[2j1n]]). OmpC has three beta-barrels associated to form a <scene name='Porin/Cv/2'>tight trimer</scene> <ref>PMID:16949612</ref>. Porin is a transmembrane protein, as can be seen from the <jmol><jmolLink><script>script "/scripts/1a0s/Hidrophobic/1.spt"; ppdiaCaptionCmd = "changeCaption('Hydrophobic residues (shown in off-white) are prevalent where the protein comes in contact with the hydrophbic layer of the double membrane, while other parts of the surface are hydrophilic (hydrophilic residues, ordered water molecules and calcium ions shown in skyblue). Shown here is the sucrose-specific porin (PDB-ID 1a0s) in its trimeric quaternary structure.','white','black');";javascript @ppdiaCaptionCmd;</script><text>hydrophobic ring</text></jmolLink></jmol> around the protein, this makes it possible to submerge in the lipid bilayer (hydrophobic amino acids are sandybrown, hydrophilic ones are cyan). As you can <scene name='1a0s/Hidrophobic1/1'>see</scene> the hole in the protein is made of mainly hydrophilic chains thus making it possible for the sugar to pass through (these scenes were created by Nádori Gergely).