Outer membrane protein G
|Outer membrane protein G (OmpG)|
|SCOPe||2iwv / SUPFAM|
Escherichia coli OmpG forms a 14-stranded beta-barrel and in contrast to most porins, appears to function as a monomer. 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 transport of larger oligosaccharides.
|This membrane protein–related article is a stub. You can help Wikipedia by expanding it.|