1.B.31 The Campylobacter jejuni Major Outer Membrane Porin (MomP) Family
Campylobacter jejuni MomP is a trimeric, β -sheet-type porin of 424 aas that packs with different lattice types when reconstituted with lipids. The protein can exist as the native trimer or as a stable monomer, depending in the concentration of sodium dodecyl sulfate. It serves several physiological functions: (1) in the structural organization of the outer membrane, (2) as an adhesin, and (3) as a porin. The monomeric and trimeric porins exhibit similar single channel conductances with the same cation selectivities and the same sensitivities to voltage when reconstituted in an artificial lipid bilayer. A second homologue of MomP with 88% identity to the first one has been sequenced (gbAL139077).
The transport reaction catalyzed by the C. jejuni MomP is:
solutes (out) solutes (periplasm)