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The Outer membrane protein G (OmpG) Family [Function: Non-specific diffusion channels] Seed alignment | Full alignment | Pfam page | Pfam Wiki page | TC-DB page

OmpG is a monomeric porin possessing a relatively large channel approximately 2.5 nm in diameter. OmpG acts as an efficient non-specific channel for mono-, di- and trisaccharides. OmpG forms a robust 14-stranded ß-barrel with a wide, nonselective pore, which exhibits voltage- and pH-dependent gating caused by loop-driven transitions.


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Literature references


Quiet Outer Membrane Protein G (OmpG) Nanopore for Biosensing
ACS Sens. 2019 May 24;4(5):1230-1235. doi: 10.1021/acssensors.8b01645. Epub 2019 Apr 25.
PMID: 30990011

A light-triggered transmembrane porin
Chem Commun (Camb). 2018 Aug 23;54(69):9623-9626. doi: 10.1039/c8cc05221b.
PMID: 30095845

The Bam complex catalyzes efficient insertion of bacterial outer membrane proteins into membrane vesicles of variable lipid composition
J Biol Chem. 2018 Feb 23;293(8):2959-2973. doi: 10.1074/jbc.RA117.000349. Epub 2018 Jan 8.
PMID: 29311257

Engineering a Novel Porin OmpGF Via Strand Replacement from Computational Analysis of Sequence Motif
Biochim Biophys Acta Biomembr. 2017 Jul;1859(7):1180-1189. doi: 10.1016/j.bbamem.2017.03.012. Epub 2017 Mar 21.
PMID: 28341438

Selective Detection of Protein Homologues in Serum Using an OmpG Nanopore
Anal Chem. 2015 Nov 3;87(21):11143-9. doi: 10.1021/acs.analchem.5b03350. Epub 2015 Oct 23.
PMID: 26451707

IR-spectroscopic characterization of an elongated OmpG mutant
Arch Biochem Biophys. 2015 Jun 15;576:73-9. doi: 10.1016/j.abb.2015.04.010. Epub 2015 May 6.
PMID: 25958106

Purification, Refolding, and Crystallization of the Outer Membrane Protein OmpG from Escherichia coli
Methods Enzymol. 2015;557:149-66. doi: 10.1016/bs.mie.2015.01.018. Epub 2015 Mar 24.
PMID: 25950964

Structure-based engineering of a minimal porin reveals loop-independent channel closure
Biochemistry. 2014 Jul 29;53(29):4826-38. doi: 10.1021/bi500660q. Epub 2014 Jul 15.
PMID: 24988371

NMR-based conformational ensembles explain pH-gated opening and closing of OmpG channel
J Am Chem Soc. 2013 Oct 9;135(40):15101-13. doi: 10.1021/ja408206e. Epub 2013 Oct 1.
PMID: 24020969

Mechanistic explanation of different unfolding behaviors observed for transmembrane and soluble ß-barrel proteins
Structure. 2013 Aug 6;21(8):1317-24. doi: 10.1016/j.str.2013.06.001. Epub 2013 Jul 3.
PMID: 23830738

Structure of outer membrane protein G by solution NMR spectroscopy
Proc Natl Acad Sci U S A. 2007 Oct 9;104(41):16140-5. doi: 10.1073/pnas.0705466104. Epub 2007 Oct 2.
PMID: 17911261

Structure of the monomeric outer-membrane porin OmpG in the open and closed conformation
EMBO J. 2006 Aug 9;25(15):3702-13. doi: 10.1038/sj.emboj.7601237. Epub 2006 Aug 3.
PMID: 16888630

Crystal structure of the monomeric porin OmpG
J Mol Biol. 2006 Jul 21;360(4):750-9. doi: 10.1016/j.jmb.2006.05.045. Epub 2006 Jun 2.
PMID: 16797588

Folding of a monomeric porin, OmpG, in detergent solution
Biochemistry. 2003 Aug 12;42(31):9453-65. doi: 10.1021/bi0344228.
PMID: 12899633

Projection structure of the monomeric porin OmpG at 6 A resolution
J Mol Biol. 2001 Jan 5;305(1):71-7. doi: 10.1006/jmbi.2000.4284.
PMID: 11114248

Biochemical and biophysical characterization of OmpG: A monomeric porin
Biochemistry. 2000 Oct 3;39(39):11845-54. doi: 10.1021/bi001065h.
PMID: 11009596

Proteins in this family with 3D-structure
View Entry
Description
Organism
Length
# strands
Major outer sheath protein
Escherichia coli (strain K12)
301
14


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