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The General Bacterial Porin (GBP-1) Family 1 [Function: Non-specific channels] Seed alignment | Full alignment in OMPdb

This family consists of the general diffusion porins from mainly the Beta and Gamma subdivisions of Proteobacteria. Although the porins of this family share common structural and functional properties with the porins of General Bacterial Porin Family 2 (GBP-2) and the Rhodobacter porin family, their sequence similarity is rather low. The porins form large aqueous channels, facilitating the diffusion of small hydrophilic molecules through the outer membrane in a non-specific manner. Important aspects of the channel activity are the conductance, the voltage dependence and the pH sensitivity. Several porins of this family have been determined at low resolution (Omp32, OmpF, Phosphoporin, OmpK36) suggesting that the 16-stranded ß-barrel is a common structural feature. In addition to that, the porins of this family seem to require trimerization in order to function properly.


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Representative image:  fam_img

Literature references

The bacterial porin superfamily: sequence alignment and structure prediction
Mol Microbiol. 1991 Sep;5(9):2153-64. doi: 10.1111/j.1365-2958.1991.tb02145.x.
PMID: 1662760

Solute uptake through general porins
Front Biosci. 2003 May 1;8:d1055-71. doi: 10.2741/1132.
PMID: 12700124

The structure of OmpF porin in a tetragonal crystal form
Structure. 1995 Oct 15;3(10):1041-50. doi: 10.1016/s0969-2126(01)00240-4.
PMID: 8589999

Crystal structures explain functional properties of two E. coli porins
Nature. 1992 Aug 27;358(6389):727-33. doi: 10.1038/358727a0.
PMID: 1380671

Crystal structures of the OmpF porin: function in a colicin translocon
EMBO J. 2008 Aug 6;27(15):2171-80. doi: 10.1038/emboj.2008.137. Epub 2008 Jul 17.
PMID: 18636093

Cation-selective pathway of OmpF porin revealed by anomalous X-ray diffraction
J Mol Biol. 2010 Feb 19;396(2):293-300. doi: 10.1016/j.jmb.2009.11.042. Epub 2009 Nov 20.
PMID: 19932117

Crystal structure of osmoporin OmpC from E. coli at 2.0 A
J Mol Biol. 2006 Oct 6;362(5):933-42. doi: 10.1016/j.jmb.2006.08.002. Epub 2006 Aug 3.
PMID: 16949612

Crystal structure of Omp32, the anion-selective porin from Comamonas acidovorans, in complex with a periplasmic peptide at 2.1 A resolution
Structure. 2000 Sep 15;8(9):981-92. doi: 10.1016/s0969-2126(00)00189-1.
PMID: 10986465

High resolution crystal structures and molecular dynamics studies reveal substrate binding in the porin Omp32
J Biol Chem. 2006 Mar 17;281(11):7413-20. doi: 10.1074/jbc.M510939200. Epub 2006 Jan 23.
PMID: 16434398

Crystal structure and functional characterization of OmpK36, the osmoporin of Klebsiella pneumoniae
Structure. 1999 Apr 15;7(4):425-34. doi: 10.1016/s0969-2126(99)80055-0.
PMID: 10196126

Structural basis for solute transport, nucleotide regulation, and immunological recognition of Neisseria meningitidis PorB
Proc Natl Acad Sci U S A. 2010 Apr 13;107(15):6811-6. doi: 10.1073/pnas.0912115107. Epub 2010 Mar 29.
PMID: 20351243

Proteins in this family with 3D-structure

S5UCA2

F2VN85

A0A0H3FYJ7

W1E8X3

E3U904

Q9ALY0

A0A0M7H8A9

Q51056

P30690

P02931

P0A264

Q8CVW1

Q9K597

P06996

P02932

P37432

Q48473

Q5RT80

E3U905

Q93K99

D6QLY0

E5G6G2

D6QLY1


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