Porin

spinqualitylabelsall models E. coli OmpC is a trimeric transmembrane protein with a porin fold (PDB code 2j1n) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Porin or Outer Membrane Proteins (Omps) act as channels which allow passive diffusion of sugars, ions and amino acids. They are beta barrel proteins which traverse the cell membrane. In E. coli they are named according to their genes: C, F, G, etc. (OmpC, OmpF, OmpG). Voltage-Dependent Anion Channel (VDAC) are ion channel Omps found in outer mitochondrial membrane. In Pseudomonas aeruginosa the porin gene products are named OprD, OprE, OprK, OprP, etc. and OpdC, OpdH, etc. Maltoporin (LamB) facilitates the diffusion of maltodextrin across the membrane. See more details in Mycobacterium tuberculosis ArfA Rv0899 for OmpA type Osmoporin OmpC (E. coli) OmpF Molecular Playground/OmpG Molecular Playground/OmpG2 Osmoporin OmpK36 (K. pneumoniae) Structure One representative porin structure is the crystal structure osmoporin OmpC from Escherichia coli (2j1n). OmpC has three beta-barrels associated to form a tight trimer . Porin is a transmembrane protein, as can be seen from the 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 see 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 Porin 3D structures

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