Porin

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== Structure ==
== Structure ==
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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).
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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 tan) are prevalent where the protein comes in contact with the hydrophbic layer of the double-layer 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).
== 3D structures of Porin ==
== 3D structures of Porin ==

Revision as of 16:26, 5 August 2023

E. coli OmpC is a trimeric transmembrane protein with a porin fold (PDB code 2j1n)

Drag the structure with the mouse to rotate

References

  1. ↑ Shoshan-Barmatz V, Israelson A, Brdiczka D, Sheu SS. The voltage-dependent anion channel (VDAC): function in intracellular signalling, cell life and cell death. Curr Pharm Des. 2006;12(18):2249-70. PMID:16787253
  2. ↑ Van Gelder P, Dumas F, Bartoldus I, Saint N, Prilipov A, Winterhalter M, Wang Y, Philippsen A, Rosenbusch JP, Schirmer T. Sugar transport through maltoporin of Escherichia coli: role of the greasy slide. J Bacteriol. 2002 Jun;184(11):2994-9. PMID:12003940
  3. ↑ Basle A, Rummel G, Storici P, Rosenbusch JP, Schirmer T. Crystal structure of osmoporin OmpC from E. coli at 2.0 A. J Mol Biol. 2006 Oct 6;362(5):933-42. Epub 2006 Aug 3. PMID:16949612 doi:10.1016/j.jmb.2006.08.002
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