The outer membranes of Gram-negative bacteria, mitochondria, and chloroplasts all contain transmembrane β-barrel proteins. These β-barrel proteins serve essential functions in cargo transport and signaling and are also vital for membrane biogenesis. They have also been adapted to perform a diverse set of important cellular functions including acting as porins, transporters, enzymes, virulence factors and receptors. Transmembrane β barrel proteins are folded into the outer membrane (OM) of Gram-negative bacteria by the β barrel assembly machinery (BAM) via a poorly understood process that occurs without known external energy sources. BAM binds the highly conserved "β signal" motif of EspP to correctly orient β strands in the OM during folding. The folding of EspP proceeds via "hybrid-barrel" intermediates in which membrane integrated β sheets are attached to the essential BAM subunit, BamA. Here you can see one of a series of structures determined by CryoEM, showing the folding intermediates of beta-barrel complexes by BamA (PDB code: 7TT5)
#molecularart ... #immolecular ... #betabarrel ... #folding ... #membrane ... #BamA ... #bacteria ... #intermediate ... #cryoem
BamA-complex structure rendered with @proteinimaging and depicted with @corelphotopaint
#molecularart ... #immolecular ... #betabarrel ... #folding ... #membrane ... #BamA ... #bacteria ... #intermediate ... #cryoem
BamA-complex structure rendered with @proteinimaging and depicted with @corelphotopaint
