Porin: Difference between revisions

No edit summary
Michal Harel (talk | contribs)
No edit summary
Line 1: Line 1:
[[Image:Ompc.png|left|250px|thumb|Crystal structure of Porin OmpC from ''E. coli'', [[2j1n]]]]
[[Image:Ompc.png|left|250px|thumb|Crystal structure of Porin OmpC from ''E. coli'', [[2j1n]]]]
{{STRUCTURE_2j1n|  PDB=2j1n  | SIZE=400| SCENE=Porin/Cv/1 |right|CAPTION=Porin OmpC from ''E. coli'', [[2j1n]] }}
{{STRUCTURE_2j1n|  PDB=2j1n  | SIZE=400| SCENE=Porin/Cv/1 |right|CAPTION=Porin OmpC from ''E. coli'', [[2j1n]] }}
[[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 (OmpC, OmpF, Ompg). See some details in [[OmpF]].  '''Voltage-Dependent Anion Channel (VDAC)''' is ion channel Omp found in outer mitochondrial membrane.  In Pseudomonas aeruginosa the porin gene products are named OprD, OprK, OprP. The images at the left and at the right correspond to one representative porin structure, ''i.e.'' 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  
[[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 (OmpC, OmpF, Ompg). See some details in [[OmpF]].  '''Voltage-Dependent Anion Channel (VDAC)''' is ion channel Omp found in outer mitochondrial membrane.  In Pseudomonas aeruginosa the porin gene products are named OprD, OprK, OprP. The images at the left and at the right correspond to one representative porin structure, ''i.e.'' 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  
<scene name='1a0s/Hidrophobic/1'>seen</scene> from the hydrophobic ring 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).
<scene name='1a0s/Hidrophobic/1'>seen</scene> from the hydrophobic ring 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).

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Alexander Berchansky, Michal Harel, Jaime Prilusky, Joel L. Sussman, Karsten Theis