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Porin (protein), the Glossary

Index Porin (protein)

Porins are beta barrel proteins that cross a cellular membrane and act as a pore, through which molecules can diffuse.[1]

Table of Contents

  1. 73 relations: Actinomycetales, Actinomycetota, Amino acid, Antibiotic, Antimicrobial resistance, Antiparallel (biochemistry), Aquaporin, Aqueous solution, Autotransporter family, Bacterial outer membrane, Beta barrel, Beta sheet, Beta turn, Campylobacter jejuni, Cell membrane, Cell wall, Chemical polarity, Chloroplast, Chloroplast membrane, Corynebacterial porin B, Cytoplasm, Dalton (unit), Diffusion, FadL outer membrane protein transport family, General bacterial porin family, Gram-negative bacteria, Gram-positive bacteria, Homotrimer, Hydrogen bond, Hydrophile, Immune response, Infection, Intermolecular force, Intimin, Ion channel, Lipid, Maltoporin, Membrane transport protein, Mitochondrion, Molecule, Monomer, Mortality rate, Mutation, Mycobacterial porin, Mycobacterium, Nuclear envelope, Nuclear pore, Nucleoporin, Nucleoside-specific porin, Oligogalacturonate-specific porin, ... Expand index (23 more) »

  2. Outer membrane proteins

Actinomycetales

The Actinomycetales is an order of Actinomycetota.

See Porin (protein) and Actinomycetales

Actinomycetota

The Actinomycetota (or Actinobacteria) are a diverse phylum of Gram-positive bacteria with high GC content.

See Porin (protein) and Actinomycetota

Amino acid

Amino acids are organic compounds that contain both amino and carboxylic acid functional groups.

See Porin (protein) and Amino acid

Antibiotic

An antibiotic is a type of antimicrobial substance active against bacteria.

See Porin (protein) and Antibiotic

Antimicrobial resistance

Antimicrobial resistance (AMR) occurs when microbes evolve mechanisms that protect them from the effects of antimicrobials (drugs used to treat infections).

See Porin (protein) and Antimicrobial resistance

Antiparallel (biochemistry)

In biochemistry, two biopolymers are antiparallel if they run parallel to each other but with opposite directionality (alignments).

See Porin (protein) and Antiparallel (biochemistry)

Aquaporin

Aquaporins, also called water channels, are channel proteins from a larger family of major intrinsic proteins that form pores in the membrane of biological cells, mainly facilitating transport of water between cells.

See Porin (protein) and Aquaporin

Aqueous solution

An aqueous solution is a solution in which the solvent is water.

See Porin (protein) and Aqueous solution

Autotransporter family

In molecular biology, an autotransporter domain is a structural domain found in some bacterial outer membrane proteins. Porin (protein) and autotransporter family are outer membrane proteins.

See Porin (protein) and Autotransporter family

Bacterial outer membrane

The bacterial outer membrane is found in gram-negative bacteria.

See Porin (protein) and Bacterial outer membrane

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).

See Porin (protein) and Beta barrel

Beta sheet

The beta sheet (β-sheet, also β-pleated sheet) is a common motif of the regular protein secondary structure.

See Porin (protein) and Beta sheet

Beta turn

β turns (also β-bends, tight turns, reverse turns, Venkatachalam turns) are the most common form of turns—a type of non-regular secondary structure in proteins that cause a change in direction of the polypeptide chain.

See Porin (protein) and Beta turn

Campylobacter jejuni

Campylobacter jejuni is a species of pathogenic bacteria that is commonly associated with poultry, and is also often found in animal feces.

See Porin (protein) and Campylobacter jejuni

Cell membrane

The cell membrane (also known as the plasma membrane or cytoplasmic membrane, and historically referred to as the plasmalemma) is a biological membrane that separates and protects the interior of a cell from the outside environment (the extracellular space).

See Porin (protein) and Cell membrane

Cell wall

A cell wall is a structural layer that surrounds some cell types, found immediately outside the cell membrane.

See Porin (protein) and Cell wall

Chemical polarity

In chemistry, polarity is a separation of electric charge leading to a molecule or its chemical groups having an electric dipole moment, with a negatively charged end and a positively charged end.

See Porin (protein) and Chemical polarity

Chloroplast

A chloroplast is a type of membrane-bound organelle known as a plastid that conducts photosynthesis mostly in plant and algal cells.

See Porin (protein) and Chloroplast

Chloroplast membrane

Chloroplasts contain several important membranes, vital for their function.

See Porin (protein) and Chloroplast membrane

Corynebacterial porin B

Porins B and C are cell wall channel-forming proteins from Corynebacterium.

See Porin (protein) and Corynebacterial porin B

Cytoplasm

In cell biology, the cytoplasm describes all material within a eukaryotic cell, enclosed by the cell membrane, except for the cell nucleus.

See Porin (protein) and Cytoplasm

Dalton (unit)

The dalton or unified atomic mass unit (symbols: Da or u) is a non-SI unit of mass defined as of the mass of an unbound neutral atom of carbon-12 in its nuclear and electronic ground state and at rest.

See Porin (protein) and Dalton (unit)

Diffusion

Diffusion is the net movement of anything (for example, atoms, ions, molecules, energy) generally from a region of higher concentration to a region of lower concentration.

See Porin (protein) and Diffusion

FadL outer membrane protein transport family

Outer membrane transport proteins (OMPP1/FadL/TodX) family includes several proteins that are involved in toluene catabolism and degradation of aromatic hydrocarbons. Porin (protein) and FadL outer membrane protein transport family are outer membrane proteins.

See Porin (protein) and FadL outer membrane protein transport family

General bacterial porin family

General bacterial porins are a family of porin proteins from the outer membranes of Gram-negative bacteria. Porin (protein) and General bacterial porin family are outer membrane proteins.

See Porin (protein) and General bacterial porin family

Gram-negative bacteria

Gram-negative bacteria are bacteria that unlike gram-positive bacteria do not retain the crystal violet stain used in the Gram staining method of bacterial differentiation.

See Porin (protein) and Gram-negative bacteria

Gram-positive bacteria

In bacteriology, gram-positive bacteria are bacteria that give a positive result in the Gram stain test, which is traditionally used to quickly classify bacteria into two broad categories according to their type of cell wall.

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Homotrimer

Trimeric form of a TNF-α mutant A homotrimer is a protein which is composed of three identical units of polypeptide.

See Porin (protein) and Homotrimer

Hydrogen bond

In chemistry, a hydrogen bond (or H-bond) is primarily an electrostatic force of attraction between a hydrogen (H) atom which is covalently bonded to a more electronegative "donor" atom or group (Dn), and another electronegative atom bearing a lone pair of electrons—the hydrogen bond acceptor (Ac).

See Porin (protein) and Hydrogen bond

Hydrophile

A hydrophile is a molecule or other molecular entity that is attracted to water molecules and tends to be dissolved by water.

See Porin (protein) and Hydrophile

Immune response

An immune response is a physiological reaction which occurs within an organism in the context of inflammation for the purpose of defending against exogenous factors.

See Porin (protein) and Immune response

Infection

An infection is the invasion of tissues by pathogens, their multiplication, and the reaction of host tissues to the infectious agent and the toxins they produce.

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Intermolecular force

An intermolecular force (IMF) (or secondary force) is the force that mediates interaction between molecules, including the electromagnetic forces of attraction or repulsion which act between atoms and other types of neighbouring particles, e.g. atoms or ions.

See Porin (protein) and Intermolecular force

Intimin

Intimin is a virulence factor (adhesin) of EPEC (e.g. E. coli O127:H6) and EHEC (e.g. E. coli O157:H7) E. coli strains.

See Porin (protein) and Intimin

Ion channel

Ion channels are pore-forming membrane proteins that allow ions to pass through the channel pore.

See Porin (protein) and Ion channel

Lipid

Lipids are a broad group of organic compounds which include fats, waxes, sterols, fat-soluble vitamins (such as vitamins A, D, E and K), monoglycerides, diglycerides, phospholipids, and others.

See Porin (protein) and Lipid

Maltoporin

Maltoporins (or LamB porins) are bacterial outer membrane proteins of the porin family. Porin (protein) and Maltoporin are outer membrane proteins.

See Porin (protein) and Maltoporin

Membrane transport protein

A membrane transport protein is a membrane protein involved in the movement of ions, small molecules, and macromolecules, such as another protein, across a biological membrane.

See Porin (protein) and Membrane transport protein

Mitochondrion

A mitochondrion is an organelle found in the cells of most eukaryotes, such as animals, plants and fungi.

See Porin (protein) and Mitochondrion

Molecule

A molecule is a group of two or more atoms held together by attractive forces known as chemical bonds; depending on context, the term may or may not include ions which satisfy this criterion.

See Porin (protein) and Molecule

Monomer

A monomer (mono-, "one" + -mer, "part") is a molecule that can react together with other monomer molecules to form a larger polymer chain or three-dimensional network in a process called polymerization.

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Mortality rate

Mortality rate, or death rate, is a measure of the number of deaths (in general, or due to a specific cause) in a particular population, scaled to the size of that population, per unit of time.

See Porin (protein) and Mortality rate

Mutation

In biology, a mutation is an alteration in the nucleic acid sequence of the genome of an organism, virus, or extrachromosomal DNA.

See Porin (protein) and Mutation

Mycobacterial porin

Mycobacterial porins are a group of transmembrane beta-barrel proteins produced by mycobacteria, which allow hydrophilic nutrients to enter the bacterium. Porin (protein) and mycobacterial porin are outer membrane proteins.

See Porin (protein) and Mycobacterial porin

Mycobacterium

Mycobacterium is a genus of over 190 species in the phylum Actinomycetota, assigned its own family, Mycobacteriaceae.

See Porin (protein) and Mycobacterium

Nuclear envelope

The nuclear envelope, also known as the nuclear membrane, is made up of two lipid bilayer membranes that in eukaryotic cells surround the nucleus, which encloses the genetic material.

See Porin (protein) and Nuclear envelope

Nuclear pore

A nuclear pore is a channel as part of the nuclear pore complex (NPC), a large protein complex found in the nuclear envelope of eukaryotic cells.

See Porin (protein) and Nuclear pore

Nucleoporin

Nucleoporins are a family of proteins which are the constituent building blocks of the nuclear pore complex (NPC).

See Porin (protein) and Nucleoporin

Nucleoside-specific porin

Nucleoside-specific porin (the tsx gene of Escherichia coli) is an outer membrane protein, Tsx, which constitutes the receptor for colicin K and Bacteriophage T6, and functions as a substrate-specific channel for nucleosides and deoxy-nucleosides. Porin (protein) and nucleoside-specific porin are outer membrane proteins.

See Porin (protein) and Nucleoside-specific porin

Oligogalacturonate-specific porin

Oligogalacturonate-specific porins (KdgM) are a family of outer bacterial membrane proteins from Dickeya dadantii. Porin (protein) and Oligogalacturonate-specific porin are outer membrane proteins.

See Porin (protein) and Oligogalacturonate-specific porin

Oligomer

In chemistry and biochemistry, an oligomer is a molecule that consists of a few repeating units which could be derived, actually or conceptually, from smaller molecules, monomers.

See Porin (protein) and Oligomer

OmpA-like transmembrane domain

OmpA-like transmembrane domain is an evolutionarily conserved domain of bacterial outer membrane proteins. Porin (protein) and OmpA-like transmembrane domain are outer membrane proteins.

See Porin (protein) and OmpA-like transmembrane domain

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. Porin (protein) and outer membrane efflux protein are outer membrane proteins.

See Porin (protein) and Outer membrane efflux protein

Outer membrane polysaccharide transporter

The extracellular polysaccharide colanic acid is produced by species of the family Enterobacteriaceae. Porin (protein) and Outer membrane polysaccharide transporter are outer membrane proteins.

See Porin (protein) and Outer membrane polysaccharide transporter

Outer membrane porin D

Outer membrane porin D is a protein family containing bacterial outer membrane porins which are involved in transport of cationic amino acids, peptides, antibiotics and other compounds. Porin (protein) and outer membrane porin D are outer membrane proteins.

See Porin (protein) and Outer membrane porin D

Outer membrane protein G

Outer membrane protein G (OmpG) is a porin, a channel proteins in the outer membrane of Gram-negative bacteria. Porin (protein) and outer membrane protein G are outer membrane proteins.

See Porin (protein) and Outer membrane protein G

Outer membrane protein W family

Outer membrane protein W (OmpW) family is a family of evolutionarily related proteins from the bacterial outer membrane. Porin (protein) and outer membrane protein W family are outer membrane proteins.

See Porin (protein) and Outer membrane protein W family

Outer membrane receptor

Outer membrane receptors, also known as TonB-dependent receptors, are a family of beta barrel proteins named for their localization in the outer membrane of gram-negative bacteria. Porin (protein) and outer membrane receptor are outer membrane proteins.

See Porin (protein) and Outer membrane receptor

Passive transport

Passive transport is a type of membrane transport that does not require energy to move substances across cell membranes.

See Porin (protein) and Passive transport

Protein

Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues.

See Porin (protein) and Protein

Protein dimer

In biochemistry, a protein dimer is a macromolecular complex or multimer formed by two protein monomers, or single proteins, which are usually non-covalently bound.

See Porin (protein) and Protein dimer

Protein primary structure

Protein primary structure is the linear sequence of amino acids in a peptide or protein.

See Porin (protein) and Protein primary structure

Protein superfamily

A protein superfamily is the largest grouping (clade) of proteins for which common ancestry can be inferred (see homology).

See Porin (protein) and Protein superfamily

Salmonella enterica

Salmonella enterica (formerly Salmonella choleraesuis) is a rod-shaped, flagellate, facultative anaerobic, Gram-negative bacterium and a species of the genus Salmonella.

See Porin (protein) and Salmonella enterica

Signal transduction

Signal transduction is the process by which a chemical or physical signal is transmitted through a cell as a series of molecular events.

See Porin (protein) and Signal transduction

Symbiogenesis

Symbiogenesis (endosymbiotic theory, or serial endosymbiotic theory) is the leading evolutionary theory of the origin of eukaryotic cells from prokaryotic organisms.

See Porin (protein) and Symbiogenesis

Translocase of the outer membrane

The translocase of the outer membrane (TOM) is a complex of proteins found in the outer mitochondrial membrane of the mitochondria. Porin (protein) and translocase of the outer membrane are outer membrane proteins.

See Porin (protein) and Translocase of the outer membrane

Transmembrane protein

A transmembrane protein is a type of integral membrane protein that spans the entirety of the cell membrane.

See Porin (protein) and Transmembrane protein

Transporter Classification Database

The Transporter Classification Database (or TCDB) is an International Union of Biochemistry and Molecular Biology (IUBMB)-approved classification system for membrane transport proteins, including ion channels. Porin (protein) and Transporter Classification Database are transmembrane proteins.

See Porin (protein) and Transporter Classification Database

Turn (biochemistry)

A turn is an element of secondary structure in proteins where the polypeptide chain reverses its overall direction.

See Porin (protein) and Turn (biochemistry)

Voltage-dependent anion channel

Voltage-dependent anion channels, or mitochondrial porins, are a class of porin ion channel located on the outer mitochondrial membrane. Porin (protein) and Voltage-dependent anion channel are outer membrane proteins.

See Porin (protein) and Voltage-dependent anion channel

White blood cell

White blood cells (scientific name leukocytes), also called immune cells or immunocytes, are cells of the immune system that are involved in protecting the body against both infectious disease and foreign invaders.

See Porin (protein) and White blood cell

X-ray crystallography

X-ray crystallography is the experimental science of determining the atomic and molecular structure of a crystal, in which the crystalline structure causes a beam of incident X-rays to diffract in specific directions.

See Porin (protein) and X-ray crystallography

See also

Outer membrane proteins

References

[1] https://en.wikipedia.org/wiki/Porin_(protein)

Also known as Nuclear pore complex proteins, Porin superfamilies, Porins, Porins and LPS.

, Oligomer, OmpA-like transmembrane domain, Outer membrane efflux protein, Outer membrane polysaccharide transporter, Outer membrane porin D, Outer membrane protein G, Outer membrane protein W family, Outer membrane receptor, Passive transport, Protein, Protein dimer, Protein primary structure, Protein superfamily, Salmonella enterica, Signal transduction, Symbiogenesis, Translocase of the outer membrane, Transmembrane protein, Transporter Classification Database, Turn (biochemistry), Voltage-dependent anion channel, White blood cell, X-ray crystallography.