Which component helps in proper folding of β-barrel membrane proteins?
Biogenesis of beta-barrel outer membrane proteins requires specialized folding and insertion systems preventing aggregation of beta-strands rich in hydrophobic residues. After Sec dependent translocation across inner membrane nascent unfolded chain enters periplasm where holdase chaperones SurA peptidyl prolyl isomerase and Skp trimeric cavity chaperone maintain unfolded state, DegP protease quality control degrades misfolded species. Targeting to BAM beta-barrel assembly machinery comprising central BamA sixteen-strand beta-barrel itself with five N-terminal POTRA domains that bind substrates
Ref: Wimley, The Versatile Beta-Barrel Membrane Protein Folding, Curr Opin Struct Biol 2003.