TCDB is operated by the Saier Lab Bioinformatics Group

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)

References associated with 1.B.31 family:

Bolla, J.M., N. Saint, G. Labesse, J.M. Pagès, and C. Dumas. (2004). Crystallization and preliminary crystallographic studies of MOMP (major outer membrane protein) from Campylobacter jejuni. Acta Crystallogr D Biol Crystallogr 60: 2349-2351. 15583387
Dé, E., M. Jullien, G. Labesse, J.M. Pagès, G. Molle, and J.M. Bolla. (2000). MOMP (major outer membrane protein) of Campylobacter jejuni; a versatile pore-forming protein. FEBS Lett. 469: 93-97. 10708763
Dhanasekar, N.N., S. Aliouane, M. Winterhalter, J.M. Pagès, and J.M. Bolla. (2017). Peptide translocation across MOMP, the major outer membrane channel from Campylobacter jejuni. Biochem Biophys Rep 11: 79-83. 28955771
Zhuang, J., A. Engel, J-M. Pages, and J.M. Bolla (1997). The Campylobacter jejuni porin trimers pack into different lattice types when reconstituted in the presence of lipid. Eur. J. Biochem. 244: 575-579. 9119026