Secondary structure of the outer membrane proteins OmpA of Escherichia coli and OprF of Pseudomonas aeruginosa.
Reads0
Chats0
TLDR
When purified without the use of ionic detergents, both OmpA and OprF proteins contained nearly 20% alpha-helical structures, which disappeared completely upon the addition of sodium dodecyl sulfate, suggesting that the proteins fold in a similar manner.Abstract:
When purified without the use of ionic detergents, both OmpA and OprF proteins contained nearly 20% alpha-helical structures, which disappeared completely upon the addition of sodium dodecyl sulfate. This result suggests that the proteins fold in a similar manner, with an N-terminal, membrane-spanning beta-barrel domain and a C-terminal, globular, periplasmic domain.read more
Citations
More filters
Journal ArticleDOI
Molecular Basis of Bacterial Outer Membrane Permeability Revisited
TL;DR: This review summarizes the development in the field since the previous review and begins to understand how this bilayer of the outer membrane can retard the entry of lipophilic compounds, owing to increasing knowledge about the chemistry of lipopolysaccharide from diverse organisms and the way in which lipopoly Saccharide structure is modified by environmental conditions.
Journal ArticleDOI
Structure of the outer membrane protein A transmembrane domain.
Alex Pautsch,Georg E. Schulz +1 more
TL;DR: The structure of the OmpA transmembrane domain consists of a regular, extended eight-stranded ß-barrel and appears to be constructed like an inverse micelle with large water-filled cavities, but does not form a pore.
Journal ArticleDOI
A molecular Swiss army knife: OmpA structure, function and expression
TL;DR: The OmpA outer membrane protein of Escherichia coli and other enterobacteria is a multifaceted protein that can function as an adhesin and invasin, participate in biofilm formation, act as both an immune target and evasin, and serves as a receptor for several bacteriophages.
Journal ArticleDOI
Preventing drug access to targets: cell surface permeability barriers and active efflux in bacteria.
TL;DR: In Gram-negative bacteria, multidrug pumps of exceptionally wide specificity frequently interact with outer membrane channels and accessory proteins, forming multisubunit complexes that extrude drug molecules directly into the medium, bypassing the outer membrane barrier.
Journal ArticleDOI
Function of pseudomonas porins in uptake and efflux.
TL;DR: The recent publication of the genomic sequence of Pseudomonas aeruginosa PAO1 has dramatically increased understanding of the porins of this organism, and these familial relationships underlie functional similarities such that well-studied members of these families become prototypes for other members.
References
More filters
Journal ArticleDOI
Circular dichroic analysis of protein conformation: inclusion of the beta-turns.
TL;DR: In this paper, the mean residue ellipticity, [theta], at any wavelength, lambda, of a protein in aqueous solution is expressed as ε = fH[theta]H infinity(1-k/n) + f beta[thet]beta + ft[thetea]t + fR[ theta]R with two constraints: 1 > or = fj > 0 and sigma fj = 1.
Journal ArticleDOI
Solubilization of the Cytoplasmic Membrane of Escherichia coli by the Ionic Detergent Sodium-Lauryl Sarcosinate
TL;DR: In this paper, the sensitivity of the outer and cytoplasmic membranes of Escherichia coli to detergent was examined by isopycnic sucrose density gradient centrifugation.
Journal ArticleDOI
Models for the structure of outer-membrane proteins of Escherichia coli derived from Raman spectroscopy and prediction methods
Horst Vogel,Fritz Jähnig +1 more
TL;DR: Folding models are developed for porin and for the segment of OmpA protein incorporated into the membrane that consists of eight amphipathic membrane-spanning beta-strands that form a beta-barrel.
Journal ArticleDOI
Pore-forming activity of OmpA protein of Escherichia coli.
Etsuko Sugawara,Hiroshi Nikaido +1 more
TL;DR: When proteoliposomes reconstituted from the purified OmpA, phospholipids, and lithium dodecyl sulfate were tested for permeability to small molecules by osmotic swelling, it was found that OMPA produced apparently nonspecific diffusion channels that allowed the penetration of various solutes.
Journal ArticleDOI
Refolding and Oriented Insertion of a Membrane Protein into a Lipid Bilayer
Thomas Surrey,Fritz Jähnig +1 more
TL;DR: This work has studied the refolding and membrane insertion of the outer membrane protein OmpA of Escherichia coli, which spontaneously refolded and inserted into the vesicle membranes.
Related Papers (5)
Models for the structure of outer-membrane proteins of Escherichia coli derived from Raman spectroscopy and prediction methods
Horst Vogel,Fritz Jähnig +1 more