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Biogenesis of β-barrel integral proteins of bacterial outer membrane

Biochemistry (Moscow), 2012
Gram-negative bacteria are enveloped by two membranes, the inner (cytoplasmic) (CM) and the outer (OM). The majority of integral outer membrane proteins are arranged in β-barrels of cylindrical shape composed of amphipathic antiparallel β-strands. In bacteria, β-barrel proteins function as water-filled pores, active transporters, enzymes, receptors ...
T F, Solov'eva   +2 more
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Bacterial ß-Barrel Outer Membrane Proteins

2009
ß-barrel outer membrane proteins constitute the second and less well-studied class of transmembrane proteins. They are present exclusively in the outer membrane of Gram-negative bacteria and presumably in the outer membrane of mitochondria and chloroplasts.
Pantelis G. Bagos, Stavros J. Hamodrakas
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Not all Bacterial Outer Membrane Proteins are β-Barrels

2023
Abstract The discovery of WzA, an octomeric helical barrel integral bacterial outer membrane protein, has challenged the widely held understanding that all integral outer membrane proteins of gram-negative bacteria are closed β-barrels composed of transmembrane β-strands.
John Heido   +5 more
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In vitro synthesized bacterial outer membrane protein is integrated into bacterial inner membranes but translocated across microsomal membranes

Nature, 1986
The LamB protein is an integral membrane protein of the outer membrane of Escherichia coli. We have now found that, when synthesized in an E. coli cell-free translation system supplemented with inverted vesicles derived from the E. coli inner membrane, LamB protein is integrated into the vesicle membrane as assayed by its resistance to extraction at ...
M, Watanabe, J F, Hunt, G, Blobel
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Protein oligomerization in the bacterial outer membrane

2009
The formation of homo-oligomeric assemblies is a well-established characteristic of many soluble proteins and enzymes. Oligomerization has been shown to increase protein stability, allow allosteric cooperativity, shape reaction compartments and provide multivalent interaction sites in soluble proteins. In comparison, our understanding of the prevalence
Guoyu, Meng   +3 more
openaire   +1 more source

The simulation approach to bacterial outer membrane proteins.

Molecular membrane biology, 2004
The outer membrane of Gram-negative bacteria serves as a protective barrier against the external environment but is rendered selectively permeable to nutrients and waste by proteins called porins. Other outer membrane proteins (OMPs) provide the membrane with a variety of other functions including active transport, catalysis, pathogenesis and signal ...
Peter J, Bond, Mark S P, Sansom
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Molecular interactions of bacterial outer membrane proteins

2004
Transport of iron-siderophores and vitamin B12 across the outer membrane (OM) of Gram-negative bacteria requires energy from the proton motive force delivered by the TonB/ExbB/ExbD complex. TonB-dependent OM receptors such as FhuA, FepA, FecA and BtuB possess a Ton box: a conserved motif located proximal to their N-terminus that has been shown to ...
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Cryo-EM Structures Reveal Multiple Stages of Bacterial Outer Membrane Protein Folding

Cell, 2022
Matthew Thomas Doyle   +2 more
exaly  

[Immunochemical study of the proteins of the bacterial membrane outer layers].

Biokhimiia (Moscow, Russia), 1981
Incubation of Micrococcus lysodeikticus protoplasts with rabbit immunoglobulins containing antibodies against micrococcal membranes and a subsequent two-dimensional immunoelectrophoresis of solubilized membrane antigens allowed to reveal four main antigens of the outer membrane, of which only two are accessible to trypsin attack.
D N, Ostrovskiĭ   +3 more
openaire   +1 more source

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