Outer Membrane Efflux Protein
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Outer Membrane Efflux Protein
The outer membrane efflux protein is a protein family member that forms trimeric (three-piece) channels allowing the export of a variety of substrates in gram-negative bacteria. Each efflux protein is composed of two repeats. The trimeric channel is composed of a 12-stranded beta-barrel that spans the outer membrane, and a long tail helical barrel that spans the periplasm. Examples include the ''Escherichia coli'' TolC outer membrane protein, which is required for proper expression of outer membrane protein genes; the Rhizobium nodulation protein; and the Pseudomonas FusA protein, which is involved in resistance to fusaric acid Fusaric acid is a picolinic acid derivative and an antibiotic (wilting agent) first isolated from the fungus '' Fusarium heterosporium''. It is typically isolated from various Fusarium species, and has been proposed for a various therapeutic appl .... References * Protein domains Protein families Outer membrane proteins {{membrane-protein ...
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Protein Family
A protein family is a group of evolutionarily related proteins. In many cases, a protein family has a corresponding gene family, in which each gene encodes a corresponding protein with a 1:1 relationship. The term "protein family" should not be confused with family as it is used in taxonomy. Proteins in a family descend from a common ancestor and typically have similar three-dimensional structures, functions, and significant sequence similarity. Sequence similarity (usually amino-acid sequence) is one of the most common indicators of homology, or common evolutionary ancestry. Some frameworks for evaluating the significance of similarity between sequences use sequence alignment methods. Proteins that do not share a common ancestor are unlikely to show statistically significant sequence similarity, making sequence alignment a powerful tool for identifying the members of protein families. Families are sometimes grouped together into larger clades called superfamilies based on st ...
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Gram-negative Bacteria
Gram-negative bacteria are bacteria that, unlike gram-positive bacteria, do not retain the Crystal violet, crystal violet stain used in the Gram staining method of bacterial differentiation. Their defining characteristic is that their cell envelope consists of a thin peptidoglycan gram-negative cell wall, cell wall sandwiched between an inner (Cytoplasm, cytoplasmic) Cell membrane, membrane and an Bacterial outer membrane, outer membrane. These bacteria are found in all environments that support life on Earth. Within this category, notable species include the model organism ''Escherichia coli'', along with various pathogenic bacteria, such as ''Pseudomonas aeruginosa'', ''Chlamydia trachomatis'', and ''Yersinia pestis''. They pose significant challenges in the medical field due to their outer membrane, which acts as a protective barrier against numerous Antibiotic, antibiotics (including penicillin), Detergent, detergents that would normally damage the inner cell membrane, and the ...
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Beta-barrel
In protein structures, a beta barrel (β barrel) is a beta sheet (β sheet) composed of tandem repeats that twists and coils to form a closed toroidal structure in which the first strand is bonded to the last strand (hydrogen bond). Beta-strands in many beta-barrels are arranged in an antiparallel fashion. Beta barrel structures are named for resemblance to the barrels used to contain liquids. Most of them are water-soluble outer membrane proteins and frequently bind hydrophobic ligands in the barrel center, as in lipocalins. Others span cell membranes and are commonly found in porins. Porin-like barrel structures are encoded by as many as 2–3% of the genes in Gram-negative bacteria. It has been shown that more than 600 proteins with various function such as oxidase, dismutase, and amylase contain the beta barrel structure. In many cases, the strands contain alternating polar and non-polar (hydrophilic and hydrophobic) amino acids, so that the hydrophobic residues are orient ...
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Bacterial Outer Membrane
The bacterial outer membrane is found in gram-negative bacteria. Gram-negative bacteria form two lipid bilayers in their cell envelopes - an inner membrane (IM) that encapsulates the cytoplasm, and an outer membrane (OM) that encapsulates the periplasm. The composition of the outer membrane is distinct from that of the inner cytoplasmic cell membrane - among other things, the outer leaflet of the outer membrane of many gram-negative bacteria includes a complex lipopolysaccharide whose lipid portion acts as an endotoxin - and in some bacteria such as ''E. coli'' it is linked to the cell's peptidoglycan by Braun's lipoprotein. Porins can be found in this layer. Outer membrane proteins Outer membrane proteins are membrane proteins with key roles associated with bacterial cell structure and morphology; cell membrane homeostasis; the uptake of nutrients; protection of the cell from toxins including antibiotics; and virulence factors including adhesins, exotoxins, and biofilm fo ...
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Periplasm
The periplasm is a concentrated gel-like matrix in the space between the inner cytoplasmic membrane and the bacterial outer membrane called the ''periplasmic space'' in Gram-negative (more accurately "diderm") bacteria. Using cryo-electron microscopy it has been found that a much smaller periplasmic space is also present in Gram-positive bacteria (more accurately "monoderm"), between cell wall and the plasma membrane. The periplasm may constitute up to 40% of the total cell volume of gram-negative bacteria, but is a much smaller percentage in gram-positive bacteria. Terminology Although bacteria are conventionally divided into two main groups—Gram-positive and Gram-negative, based upon their Gram-stain retention property—this classification system is ambiguous as it can refer to three distinct aspects (staining result, cell-envelope organization, taxonomic group), which do not necessarily coalesce for some bacterial species. In most situations such as in this article, Gram ...
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Escherichia Coli
''Escherichia coli'' ( )Wells, J. C. (2000) Longman Pronunciation Dictionary. Harlow ngland Pearson Education Ltd. is a gram-negative, facultative anaerobic, rod-shaped, coliform bacterium of the genus '' Escherichia'' that is commonly found in the lower intestine of warm-blooded organisms. Most ''E. coli'' strains are part of the normal microbiota of the gut, where they constitute about 0.1%, along with other facultative anaerobes. These bacteria are mostly harmless or even beneficial to humans. For example, some strains of ''E. coli'' benefit their hosts by producing vitamin K2 or by preventing the colonization of the intestine by harmful pathogenic bacteria. These mutually beneficial relationships between ''E. coli'' and humans are a type of mutualistic biological relationship—where both the humans and the ''E. coli'' are benefitting each other. ''E. coli'' is expelled into the environment within fecal matter. The bacterium grows massi ...
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Fusaric Acid
Fusaric acid is a picolinic acid derivative and an antibiotic (wilting agent) first isolated from the fungus '' Fusarium heterosporium''. It is typically isolated from various Fusarium species, and has been proposed for a various therapeutic applications. However, it is primarily used as a research tool. Its mechanism of action is not well understood. It likely inhibits Dopamine beta-hydroxylase (the enzyme that converts dopamine to norepinephrine). It may also have other actions, such as the inhibition of cell proliferation and DNA synthesis. Fusaric acid and analogues also reported as quorum sensing In biology, quorum sensing or quorum signaling (QS) is the process of cell-to-cell communication that allows bacteria to detect and respond to cell population density by gene regulation, typically as a means of acclimating to environmental disadv ... inhibitors.Tung et al., Eur. J. Med. Chem. https://dx.doi.org/10.1016/j.ejmech.2016.11.044. It is used to make bupicomide. Refe ...
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Protein Domains
In molecular biology, a protein domain is a region of a protein's polypeptide chain that is self-stabilizing and that folds independently from the rest. Each domain forms a compact folded three-dimensional structure. Many proteins consist of several domains, and a domain may appear in a variety of different proteins. Molecular evolution uses domains as building blocks and these may be recombined in different arrangements to create proteins with different functions. In general, domains vary in length from between about 50 amino acids up to 250 amino acids in length. The shortest domains, such as zinc fingers, are stabilized by metal ions or disulfide bridges. Domains often form functional units, such as the calcium-binding EF hand domain of calmodulin. Because they are independently stable, domains can be "swapped" by genetic engineering between one protein and another to make chimeric proteins. Background The concept of the domain was first proposed in 1973 by Wetlaufer after ...
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Protein Families
A protein family is a group of evolutionarily related proteins. In many cases, a protein family has a corresponding gene family, in which each gene encodes a corresponding protein with a 1:1 relationship. The term "protein family" should not be confused with family as it is used in taxonomy. Proteins in a family descend from a common ancestor and typically have similar three-dimensional structures, functions, and significant sequence similarity. Sequence similarity (usually amino-acid sequence) is one of the most common indicators of homology, or common evolutionary ancestry. Some frameworks for evaluating the significance of similarity between sequences use sequence alignment methods. Proteins that do not share a common ancestor are unlikely to show statistically significant sequence similarity, making sequence alignment a powerful tool for identifying the members of protein families. Families are sometimes grouped together into larger clades called superfamilies based on stru ...
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