2022年2月11日 · Outer membrane proteins (OMPs), located on the outer membrane of gram-negative bacteria, have a β-strand structure and form nanopores, which allow passage of ions, sugars, and small...

OmpG, a monomeric pore-forming protein from Escherichia coli outer membranes, was refolded from inclusion bodies and crystallized in two different conformations. The OmpG channel is a 14-stranded β-barrel, with short periplasmic turns and seven extracellular loops. Crystals grown at neutral pH show the channel in the open state at 2.3 Å ...

Outer membrane protein G (OmpG) is a porin, a channel proteins in the outer membrane of Gram-negative bacteria. Escherichia coli OmpG forms a 14-stranded beta-barrel and in contrast to most porins, appears to function as a monomer. [1] .

2022年5月18日 · Outer membrane protein G (OmpG) nanopores have advantages for single-molecule sensing owing to their rigid monomeric structure, which comprises seven flexible loops, providing distinct gating patterns upon analyte binding.

2008年4月29日 · OmpG is a monomeric porin from the outer membrane of Escherichia coli that presents an attractive alternative to αHL for stochastic sensing (4–7). Previous studies have shown that OmpG undergoes pH-dependent, voltage-dependent, and spontaneous gating (4, 5).

2017年12月12日 · Nature Communications - Porins, like OmpG, are embedded in the outer membrane of bacteria and facilitate uptake and secretion of nutrients and ions. Here the authors present a protocol for solid...

OmpG是一种来自大肠杆菌外膜的单体成孔蛋白，可以从包涵体中折叠出来，并以两种不同的构象进行结晶。OmpG通道为14链β桶，具有短的周质转弯和七个细胞外环。在中性pH下生长的晶体在2.3 A分辨率下显示通道处于打开状态。

2006年7月21日 · All porins of Gram-negative bacteria that have been crystallized to date form stable trimers, with each monomer composed of a 16-stranded β-barrel with a relatively narrow central pore. In contrast, the OmpG porin is unique, as it appears to function as a monomer.

2023年2月6日 · Outer Membrane Protein G (OmpG), a monomeric porin possessing seven functionalizable loops, has been reported as an effective sensing platform for selective protein detection. Using flow cytometry to screen unfavorable constructs, we identified two OmpG nanopores with unique peptide motifs displayed in either loop 3 or 6, which also exhibited ...

2024年12月3日 · OmpG is an efficient, nonspecific channel for mono-, di, and trisaccharides with sizes less than 600 Daltons although liposome swelling assays have demonstrated that OmpG is capable of transporting large solutes . [More information is available at EcoCyc: G6657].