Target type: molecularfunction
Enables the transfer of substances, sized less than 1000 Da, from one side of a membrane to the other. The transmembrane portions of porins consist exclusively of beta-strands which form a beta-barrel. They are found in the outer membranes of Gram-negative bacteria, mitochondria, plastids and possibly acid-fast Gram-positive bacteria. [GOC:mtg_transport, ISBN:0815340729, PMID:10839820, TC:1.B.1.-.-]
Porin activity is a fundamental molecular function in cellular biology, mediating the passive diffusion of small molecules across biological membranes. Porins are integral membrane proteins that form channels through the outer membrane of bacteria, mitochondria, and chloroplasts. These channels are typically selective for specific molecules, often based on size and charge.
The molecular mechanism of porin activity involves several key features:
1. **Channel Formation:** Porins assemble into multimeric structures, forming water-filled channels that span the outer membrane. These channels provide a hydrophilic pathway for the passage of small molecules, bypassing the hydrophobic barrier of the membrane.
2. **Size and Charge Selectivity:** The pore size and amino acid residues lining the channel confer selectivity for specific molecules. Smaller molecules, such as sugars, ions, and amino acids, can readily pass through the channel, while larger molecules are excluded. Similarly, the charge distribution within the channel can influence the passage of charged molecules.
3. **Passive Diffusion:** Porin activity relies on passive diffusion, driven by the concentration gradient of the transported molecule. Molecules move from an area of high concentration to an area of low concentration without the need for energy expenditure.
4. **Regulation:** In some cases, porin activity can be regulated by factors such as pH, membrane potential, or the binding of specific ligands. These regulatory mechanisms allow cells to control the flow of molecules across the outer membrane in response to environmental changes.
Porin activity plays a crucial role in a variety of cellular processes, including:
* **Nutrient uptake:** Porins facilitate the uptake of essential nutrients, such as sugars, amino acids, and vitamins.
* **Waste excretion:** They also allow the removal of waste products from the cell.
* **Signal transduction:** Some porins can act as receptors for specific signaling molecules, transmitting information across the outer membrane.
* **Antibiotic resistance:** In bacteria, porins can contribute to antibiotic resistance by allowing the efflux of antibiotics from the cell.
In summary, porin activity is a crucial process that enables the controlled movement of small molecules across biological membranes. This function is essential for maintaining cellular homeostasis, nutrient uptake, waste excretion, and other vital processes.'
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Protein | Definition | Taxonomy |
---|---|---|
Bcl-2 homologous antagonist/killer | A Bcl-2 homologous antagonist/killer that is encoded in the genome of human. [PRO:WCB, UniProtKB:Q16611] | Homo sapiens (human) |
Voltage-dependent anion-selective channel protein 2 | A voltage-dependent anion-selective channel protein 2 that is encoded in the genome of human. [PRO:DNx, UniProtKB:P45880] | Homo sapiens (human) |
Compound | Definition | Classes | Roles |
---|---|---|---|
alexidine dihydrchloride | |||
6-n-tridecylsalicylic acid | 6-n-tridecylsalicylic acid: structure given in first source | hydroxybenzoic acid | |
5,6-dehydrokawain | 5,6-dehydrokawain: from Alpinia speciosa rhizoma; RN given for cpd without isomeric designation; structure given in first source | 2-pyranones; aromatic ether | |
erastin | erastin : A member of the class of quinazolines that is quinazolin-4(3H)-one in which the hydrogens at positions 2 and 3 are replaced by 1-{4-[(4-chlorophenoxy)acetyl]piperazin-1-yl}ethyl and 2-ethoxyphenyl groups, respectively. It is an inhibitor of voltage-dependent anion-selective channels (VDAC2 and VDAC3) and a potent ferroptosis inducer. erastin: an antineoplastic agent; structure in first source | aromatic ether; diether; monochlorobenzenes; N-acylpiperazine; N-alkylpiperazine; quinazolines; tertiary carboxamide | antineoplastic agent; ferroptosis inducer; voltage-dependent anion channel inhibitor |
abt-737 | aromatic amine; aryl sulfide; biphenyls; C-nitro compound; monochlorobenzenes; N-arylpiperazine; N-sulfonylcarboxamide; secondary amino compound; tertiary amino compound | anti-allergic agent; anti-inflammatory agent; antineoplastic agent; apoptosis inducer; B-cell lymphoma 2 inhibitor | |
meiogynin a | meiogynin A: from the bark of Meiogyne cylindrocarpa; structure in first source | ||
jy-1-106 | JY-1-106: a BH3 alpha-helix mimetic that functions as a pan-Bcl-2 inhibitor; structure in first source |