Porin
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 more details in
| |||||||||
| Porin OmpC trimer from E. coli, 2j1n | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||||
| |||||||||
| |||||||||
| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
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 [1]. Porin is a transmembrane protein, as can be 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 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).
PorinPorin
Updated on 09-October-2013
2xe5, 2xe1, 2xe2, 2xe3, 2j1n – EcOmpC – Escherichia coli
3k19, 3k1b, 2zfg, 1omf, 2omf, 1opf, 3poq, 3pou, 3pox – EcOmpF
3nb3 – EcOmpA + EcOmpC - EM
3upg, 3uu2 – OmpC – Salmonella enterica
1hxt, 1hxu, 1hxx, 1bt9, 1gfm, 1gfn, 1gfo, 1gfp, 1gfq, 1mpf – EcOmpF (mutant)
2iwv, 2iww, 2f1c - EcOmpG
2x9k - EcOmpG (mutant)
2wjq, 2wjr – EcOmp NANC
1pho - EcOmp
3a2r – NmOmpB – Neisseria meningitides
3sy9 – PaOpdC – Pseudomonas aeruginosa
2odj, 3sy7, 4foz – PaOprD
3szd - PaOpdF
3t20 – PaOpdH
2qtk, 2y2x, 3sys – PaOpdK
3t0s - PaOpdL
2y0k, 2y0l, 3szv – PaOpdO
3syb – PaOpdP
3t24 - PaOpdQ
3jty – Omp – Pseudomonas fluorescens
2v9u – MsOmp rim domain – Mycobacteria smegmatis
1uun – MsOmp (mutant)
2fgr - DaOmp32 - Delftia acidovorans
1a0s, 1mpr - StOmp - Salmonella typhimurium
3nsg - StOmpF
2prn, 1bh3, 3prn, 5prn, 6prn, 7prn, 8prn – RbOmp (mutant) - Rhodopseudomonas blastica
1prn - RbOmp
1osm – OmpK36 – Klebsiella pneumoniae
2por, 3por – Omp – Rhodobacter capsulatus
4aui – Omp – Neisseria gonorrheae
4gey, 4gf4 – Omp B – Pseudomonas putida
Porin + polypeptidesPorin + polypeptides
2j4u - EcOmpC + lactotransferrin fragment
2zld - EcOmpF + colicin E3
3o0e - EcOmpF + colicin peptide
1h6s - RbOmp + inserted sequence
Porin + various compoundsPorin + various compounds
3hw9, 3hwb - EcOmpF + ions
3fyx - Ec~OmpF + dibenzo-18-crown-6
4gcp, 4gcq, 4gcs – EcOmpF + antibiotic
1af6, 1mpq, 1mpm, 1mpn, 1mpo - EcOmp LAMB + sugars
3a2s, 3a2t - NmOmpB + sugars
3a2u - NmOmpB + AMPPNP
2o4v - PaOprP + phosphate
2fgq - DaOmp32 + malate
1e54 - Omp32 + sulfate - Comamonas acidovorans
1oh2, 1a0t - StOmp + sucrose
Voltage-Dependent Anion ChannelVoltage-Dependent Anion Channel
2jk4 – hVDAC-1 – human
2k4t - hVDAC-1 - NMR
3emn – VDAC-1 - mouse
ReferencesReferences
- ↑ 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