1.B.21 The OmpG Porin (OmpG) Family
The OmpG family consists of two distantly related functionally characterized E. coli proteins, OmpG and OmpL. The OmpG channel appears to be much larger than the E. coli OmpC or OmpF channels (estimated limited diameter of about 2 nm) (Fajardo et al., 1998). The channel lacks solute specificity, and a folding model suggests a 16-stranded β-barrel porin lacking the large external loop, L3, that constricts the pores in other porins. However, Liang and Tamm (2007) found a 14-stranded β-barrel based on NMR analyses. OmpG has been reconstituted in planar bilayers where it exhibits uniform sized channels. Results suggested that OmpG forms a monomeric rather than the usual trimeric porin (Conlan et al., 2000). The pH-gating conformations of the beta-barrel have been solved. When the pH changes from neutral to acidic, the flexible extracellular loop L6 folds into and closes the OmpG pore (Damaghi et al. 2010).
Voltage-induced closure occurred in a single step, and channel block by Gd3+ lacked cooperativity seen with trimeric porin OmpF. Incorporation of OmpG into lipid membranes revealing protein-lipid interactions and β-barrel orientation, as sudied by Anbazhagan et al. (2008). OmpG has been intensively studied using physical approaches, providing data on its possible structure and biogenesis (Damaghi et al., 2010; Korkmaz-Ozkan et al., 2010). Refolding pathways of the sequential β-hairpins and kinetics of OmpG folding have been reported (Damaghi et al., 2011).
OmpL has been purified and reconstituted. It allowed diffusion of small solutes including sugars (Dartigalongue et al., 2000). Contrary to an earlier report, it does not influence Dsb-mediated redox potential in the periplasm (Sardesai et al., 2003). The OmpG family is related to the Cyclodextrin Porin (CDP; 1.B.26) and the Oligogalacturonate Porin (KdgM; 1.B.35) families (Condemine et al., 2005).