Suchergebnisse
12. Feb. 2023 · FkpA maintains a larger fraction of OmpA 171 in an unfolded state at intermediate timepoints (5–10 min) and decreases the elusive population throughout the folding reaction (Figure S3a), indicating that FkpA suppresses some lipid-induced aggregation.
8. Feb. 2024 · A network of periplasmic chaperones that includes SurA, Skp, and FkpA binds unfolded OMPs (uOMPs) in dynamic conformational ensembles to suppress uOMP aggregation and promote proper OMP folding and function.
We recently identified FkpA by selecting for the in-creased yield of antibody single-chain Fv (scFv) frag-ments in phage display, even of those not containing cis-prolines. We have now investigated the properties of FkpA in vitro. The peptidylprolyl cis-trans-isomerase ac-tivity of FkpA was found to be among the highest of any
10. Sept. 2013 · To determine whether FkpA plays a direct role in OMP biogenesis, we performed affinity copurifications using C-terminally His-tagged FkpA expressed from a multicopy plasmid, pBAD-FkpA-His 6, in ΔfkpA cells to capture those FkpA-interacting proteins in cells.
2. Nov. 2022 · Here we find that the chaperone FkpA enhances outer membrane protein folding and tightly binds its clients with an extensive interaction interface. This modified holdase function of FkpA distinguishes it from other periplasmic chaperones and complements their functions to ensure robust outer membrane biogenesis.
1. Aug. 2014 · FkpA is a V-shaped homodimer composed of two subunits of 245 residues (Fig. 5). Each monomer can be divided into two domains, a N-terminal domain made up of three helices and a C-terminal domain responsible for the PPIase activity.
13. Apr. 2010 · As Skp and FkpA are both molecular chaperones with general ability to refold misfolded proteins and prevent their aggregation into insoluble inclusion bodies in the periplasm, the soluble and insoluble scFvD1.3 yields in the Skp/scFvD1.3 and FkpA/scFvD1.3 cells were examined with Western blot.
