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The Campylobacter major outer membrane protein Family [Function: Non-specific diffusion channels] Seed alignment | Full alignment | Pfam page | TC-DB page

Campylobacter jejuni Major Outer Membane Protein (MomP) is possibly a ß-barrel porin, which displays two folded structures: a classical oligomer and a monomer showing similar channel properties (conductance and cation selectivity). MomP is a multifunction surface protein, since it has a triple role: porin activity, it is involved in the structural organization of the outer membrane, and acts as an adhesin. The 2.1-Å resolution structure of recombinant MOMP showed that although the protein has timeric arrangement similar to OmpC, it is an 18-stranded, not 16-stranded, ß-barrel.

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Literature references

Crystallization and preliminary crystallographic studies of MOMP (major outer membrane protein) from Campylobacter jejuni
Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 2):2349-51. doi: 10.1107/S0907444904024795. Epub 2004 Nov 26.
PMID: 15583387

Sequence polymorphism, predicted secondary structures, and surface-exposed conformational epitopes of Campylobacter major outer membrane protein
Infect Immun. 2000 Oct;68(10):5679-89. doi: 10.1128/iai.68.10.5679-5689.2000.
PMID: 10992471

MOMP (major outer membrane protein) of Campylobacter jejuni; a versatile pore-forming protein
FEBS Lett. 2000 Mar 3;469(1):93-7. doi: 10.1016/s0014-5793(00)01244-8.
PMID: 10708763

Campylobacter jejuni major outer membrane protein and a 59-kDa protein are involved in binding to fibronectin and INT 407 cell membranes
FEMS Microbiol Lett. 1997 Dec 15;157(2):233-8. doi: 10.1111/j.1574-6968.1997.tb12778.x.
PMID: 9435102

The Campylobacter jejuni porin trimers pack into different lattice types when reconstituted in the presence of lipid
Eur J Biochem. 1997 Mar 1;244(2):575-9. doi: 10.1111/j.1432-1033.1997.t01-1-00575.x.
PMID: 9119026

Proteins in this family with 3D-structure
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