PR00183

ECOLIPORIN

PRINTS entry
Member databasePRINTS
PRINTS typefamily
Short nameECOLIPORIN

Description
Imported from IPR001897

Porins are found in the outer membranes of Gram-negative bacteria, mitochondria and chloroplasts, where they form ion-selective channels for small hydrophilic molecules (up to ~600 D)
[1, 2]
. X-ray structure analyses of several bacterial porins
[3, 4, 5]
have revealed a 16-stranded anti-parallel β-barrel structure enclosing the transmembrane pore, by contrast with all other integral membrane proteins described to date, which are α-helical. Three subunits form a trimer; the 3-fold axis is approximately parallel to the barrel axes and is assumed to be perpendicular to the membrane plane.

From the range of porins now known, similarities have been observed between porins from different species, and between porins of different specificity within the same species. But most porins cannot be related to each other on the basis of sequence alone, and this is reflected in the lengths of the known porin sequences, which range from 282-483 residues/monomer.

This entry is specific for porins in the gammaproteobacteria.

References
Imported from IPR001897

1.Biophysics of the structure and function of porins. Jap BK, Walian PJ. Q. Rev. Biophys. 23, 367-403, (1990). PMID: 2178269

2.Porins and specific channels of bacterial outer membranes. Nikaido H. Mol. Microbiol. 6, 435-42, (1992). View articlePMID: 1373213

3.The structure of porin from Rhodobacter capsulatus at 1.8 A resolution. Weiss MS, Kreusch A, Schiltz E, Nestel U, Welte W, Weckesser J, Schulz GE. FEBS Lett. 280, 379-82, (1991). View articlePMID: 1707373

4.A common channel-forming motif in evolutionarily distant porins. Pauptit RA, Schirmer T, Jansonius JN, Rosenbusch JP, Parker MW, Tucker AD, Tsernoglou D, Weiss MS, Schultz GE. J. Struct. Biol. 107, 136-45, (1991). View articlePMID: 1725488

5.Refined structure of the porin from Rhodopseudomonas blastica. Comparison with the porin from Rhodobacter capsulatus. Kreusch A, Schulz GE. J. Mol. Biol. 243, 891-905, (1994). View articlePMID: 7525973

Supplementary References

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