Background: The inner membrane-anchored periplasmic folding factor PpiD is described as a parvulin-like peptidyl prolyl isomerase (PPIase) that assists in the maturation of the major beta-barrel outer membrane proteins (OMPs) of Escherichia coli. More recent work however, calls these findings into question. Here, we re-examined the role of PpiD in the E.
View Article and Find Full Text PDFInt J Med Microbiol
November 2010
The Escherichia coli periplasmic chaperone and peptidyl-prolyl isomerase (PPIase) SurA is a major factor in the biogenesis of β-barrel outer membrane proteins (OMPs) and as such plays an integral role in cell envelope homeostasis and cell envelope functions. Recently, the biological importance of SurA was further substantiated by the finding that SurA also affects pathogenicity, being required for full virulence of uropathogenic Escherichia coli, Salmonella, and Shigella spp. Moreover, given the conservation of the protein, SurA likely plays similar roles in other Gram-negative bacteria and may hence prove a valuable drug target against Gram-negative pathogens.
View Article and Find Full Text PDFThe basic biochemical and biophysical principles by which chaperone-bound membrane proteins are targeted to the outer membrane of Gram-negative bacteria for insertion and folding are unknown. Here we compare spontaneous folding of outer membrane protein A (OmpA) of Escherichia coli from its urea-unfolded form and from the complex with its periplasmic chaperone Skp into lipid bilayers. Skp facilitated folding of OmpA into negatively charged membranes containing dioleoylphosphatidylglycerol (DOPG).
View Article and Find Full Text PDFPeriplasmic Skp facilitates folding and membrane insertion of many outer membrane proteins (OMPs) into the outer membrane of Gram-negative bacteria. We have examined the binding sites of outer membrane protein A (OmpA) from Escherichia coli in its complexes with the membrane protein chaperone Skp and with Skp and lipopolysaccharide (LPS) by site-directed fluorescence spectroscopy. Single-Trp OmpA mutants, W(n)-OmpA, with tryptophan at position n in the polypeptide chain were isolated in the unfolded form in 8 M urea.
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