نتایج جستجو برای: bacterial outer membrane proteins
تعداد نتایج: 1053377 فیلتر نتایج به سال:
To fulfill their nutritional requirement for iron, bacteria utilize various iron sources which include the host proteins transferrin and lactoferrin, heme, and low molecular weight iron chelators termed siderophores. The iron sources are transported into the Gram-negative bacterial cell via specific uptake pathways which include an outer membrane receptor, a periplasmic binding protein (PBP), a...
Surface display of heterologous proteins or polypeptides on the surface of bacteria has gained momentum in recent years. Until recently, arrays of anchors or carriers have been identified for displaying diverse passenger proteins on the surface of Escherichia coli, majority of these involving the outer membrane proteins (OMPs). The reason for opting outer membrane proteins lies mainly i n its a...
OprM with a M(r) of 49 K is associated with the multidrug resistance of Pseudomonas aeruginosa. Detergent fractionation of bacterial cells has demonstrated that OprM is located in the outer membrane from which it sediments with the other major outer membrane proteins. In this study we have determined the location of OprM as the P. aeruginosa outer membrane. Western immunoblots of cell fractions...
Typically, the redox proteins of respiratory chains in Gram-negative bacteria are localized in the cytoplasmic membrane or in the periplasm. An alternative arrangement appears to be widespread within the betaproteobacterial genus Neisseria, wherein several redox proteins are covalently associated with the outer membrane. In the present paper, we discuss the structural properties of these outer ...
The biogenesis of membranes from constituent proteins and lipids is a fundamental aspect of cell biology. In the case of proteins assembled into bacterial outer membranes, an overarching question concerns how the energy required for protein insertion and folding is accessed at this remote location of the cell. The translocation and assembly module (TAM) is a nanomachine that functions in outer ...
0022-2836/$ see front matter © 2007 E Spontaneous membrane insertion and folding of β-barrel membrane proteins from an unfolded state into lipid bilayers has been shown previously only for few outermembrane proteins of Gram-negative bacteria. Here we investigated membrane insertion and folding of a human membrane protein, the isoform 1 of the voltage-dependent anion-selective channel (hVDAC1) o...
The current topological model for the Escherichia coli outer membrane protein OmpA predicts eight N-terminal transmembrane segments followed by a long periplasmic tail. Several recent reports have raised serious doubts about the accuracy of this prediction. An alternative OmpA model has been constructed using (1) computer-aided predictions developed specifically to predict topology of bacterial...
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