Molecular Playground/OmpG: Difference between revisions

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==Structural Features of OmpG==
==Structural Features of OmpG==
OmpG is a 14-stranded beta-barrel and in contrast to most porins, appears to function as a monomer.[1] The central pore of OmpG is wider than other E. coli porins and it is speculated that it may form a non-specific channel for the passive transport of larger oligosaccharides.[1] OmpG adopts two conformations: open and closed. At neutral pH the porin displays an open conformation. However at a more acidic pH the closed conformation is adopted. This closed conformation is a result of OmpG's flexible extracellular loop 6, which folds across the channel blocking the pore opening.  The rearrangement of loop 6 appears to be triggered by a pair of histidine residues, which repel one another at acidic pH, resulting in the breakage of neighbouring H-bonds and a lengthening of loop 6 from 10 to 17 residues[2,3]. <scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/3'></scene>
OmpG is a 14-stranded beta-barrel and in contrast to most porins, appears to function as a monomer.[1] The central pore of OmpG is wider than other E. coli porins and it is speculated that it may form a non-specific channel for the passive transport of larger oligosaccharides.[1] OmpG adopts two conformations: open and closed. At neutral pH the porin displays an open conformation. However at a more acidic pH the closed conformation is adopted. This closed conformation is a result of OmpG's flexible extracellular loop 6, which folds across the channel blocking the pore opening.  The rearrangement of loop 6 appears to be triggered by a pair of histidine residues, which repel each another at acidic pH, resulting in the breakage of neighbouring H-bonds and a lengthening of loop 6 from 10 to 17 residues[2,3]. <scene name='User:Christina_Chisholm/Sandbox_1/Greenwoselection_ompg/3'></scene>


[[Image:OmpG Conformation.png|thumb|]]
[[Image:OmpG Conformation.png|thumb|]]
[2IWW]
[2IWW]
[http://en.wikipedia.org/wiki/Outer_membrane_protein_G].
[http://en.wikipedia.org/wiki/Outer_membrane_protein_G].
The loop environment of OmpG carries a net negative charge.  This highly negative character may be implicated in the gating behavior of OmpG.  If we can gain a deeper understanding of OmpG gating, we could could use this knowledge to tune it for specific detection of target analytes. 
==Current OmpG Projects in the Chen Lab==
Engineering loop 6 to detect large protein analytes
Investigating the effect of loop charge on the gating behavior of OmpG


==Additional Resources==
==Additional Resources==

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Christina Chisholm, Bib Yang, Monifa Fahie, Michal Harel