| Gram-negative porin | |||||||||
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| Identifiers | |||||||||
| Symbol | Porin_08134891516 | ||||||||
| Pfam | PF00267 | ||||||||
| Pfam clan | CL0193 | ||||||||
| InterPro | IPR001702 | ||||||||
| PROSITE | PDOC00498 | ||||||||
| SCOP2 | 1mpf /SCOPe /SUPFAM | ||||||||
| TCDB | 1.B.1 | ||||||||
| OPM superfamily | 31 | ||||||||
| OPM protein | 1pho | ||||||||
| CDD | cd01345 | ||||||||
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Porins arebeta barrelproteins that cross acellular membrane and act as a pore, through whichmolecules candiffuse.[1] Unlike othermembrane transport proteins, porins are large enough to allowpassive diffusion, i.e., they act aschannels that are specific to different types of molecules. They are present in theouter membrane ofgram-negative bacteria and somegram-positivemycobacteria (mycolic acid-containingactinomycetes), the outer membrane ofmitochondria, and theouter chloroplast membrane (outer plastid membrane).
Porins are composed ofbeta sheets (β sheets) made up ofbeta strands (β strands) which are linked together bybeta turns (β turns) on thecytoplasmic side and longloops ofamino acids on the other. The β strands lie in anantiparallel fashion and form a cylindrical tube, called abeta barrel (β barrel).[2] The amino acid composition of the porin β strands are unique in that polar and nonpolar residues alternate along them. This means that the nonpolar residues face outward so as to interact with thenonpolarlipids ofouter membrane, whereas the polar residues face inwards into the center of the beta barrel to create theaqueous channel. The specific amino acids in the channel determine the specificity of the porin to different molecules.
The β barrels that make up a porin are composed of as few as eight β strands to as many as twenty-two β strands. The individual strands are joined together by loops and turns.[3] The majority of porins aremonomers; however, somedimeric porins have been discovered, as well as anoctameric porin.[4] Depending on the size of the porin, the interior of the protein may either be filled with water, have up to two β strands folded back into the interior, or contain a "stopper" segment composed of β strands.
All porins formhomotrimers in the outer membrane, meaning that three identical porin subunits associate together to form a porin super-structure with three channels.[5]Hydrogen bonding anddipole-dipole interactions between each monomer in the homotrimer ensure that they do not dissociate, and remain together in the outer membrane.
Several parameters have been used to describe the structure of a porin protein. They include the tilting angle (α), shear number (S), strand number (n), and barrel radius (R).[6] The tilting angle refers to the angle relative to the membrane. The shear number (S) is the number of amino acid residues found in each β strands. Strand number (n) is the amount of β strands in the porin, and barrel radius (R) refers to the radius of the opening of the porin. These parameters are related via the following formulas:
and,
Using these formulas, the structure of a porin can be determined by knowing only a few of the available parameters. While the structure of many porins have been determined usingX-ray crystallography, the alternative method of sequencingprotein primary structure may also be used instead.
Porins are water-filled pores and channels found in the membranes of bacteria and eukaryotes. Porin-like channels have also been discovered in archaea.[7] Note that the term "nucleoporin" refers to unrelated proteins that facilitate transport throughnuclear pores in thenuclear envelope.
Porins are primarily involved in passively transportinghydrophilic molecules of various sizes and charges across the membrane.[8] For survival, certain required nutrients and substrates must be transported into the cells. Likewise, toxins and wastes must be transported out to avoid toxic accumulation.[9] Additionally, porins can regulate permeability and prevent lysis by limiting the entry of detergents into the cell.[8]
Two types of porins exist to transport different materials– general and selective. General porins have no substrate specificities, though some exhibit slight preferences for anions or cations.[8] Selective porins are smaller than general porins, and have specificities for chemical species. These specificities are determined by the threshold sizes of the porins, and the amino acid residues lining them.[5]
Ingram-negative bacteria, the inner membrane is the major permeability barrier.[10] The outer membrane is more permeable to hydrophilic substances, due to the presence of porins.[5] Porins have threshold sizes of transportable molecules that depend on the type of bacteria and porin. Generally, only substances less than 600daltons in size can diffuse through.[8]
Porins were first discovered in gram-negative bacteria, butgram-positive bacteria with both types of porins have been found.[9] They exhibit similar transport functions but have a more limited variety of porins, compared to the distribution found in gram-negative bacteria.[9] Gram-positive bacteria lack outer membranes, so these porin channels are instead bound to specific lipids within thecell walls.[7]
Porins are also found in eukaryotes, specifically in the outer membranes ofmitochondria andchloroplasts.[9][10] The organelles contain general porins that are structurally and functionally similar to bacterial ones. These similarities have supported theEndosymbiotic theory, through which eukaryotic organelles arose from gram-negative bacteria.[10] However, eukaryotic porins exhibit the same limited diversity as gram-positive porins, and also display a greater voltage-dependent role during metabolism.[9][10]
Archaea also contain ion channels that have originated from general porins.[7] The channels are found in the cell envelope and help facilitate solute transfer. They have similar characteristics as bacterial and mitochondrial porins, indicating physiological overlaps over all three domains of life.[7]
Many porins are targets for hostimmune cells, resulting insignaling pathways that lead to bacterial degradation. Therapeutic treatments, like vaccinations andantibiotics, are used to supplement thisimmune response.[5] Specific antibiotics have been designed to travel through porins in order to inhibit cellular processes.[8]
However, due to selective pressure, bacteria can develop resistance throughmutations in the porin gene.[5] The mutations may lead to a loss of porins, resulting in the antibiotics having a lower permeability or being completely excluded from transport. These changes have contributed to the global emergence ofantibiotic resistance, and an increase inmortality rates frominfections.[5]
The discovery of porins has been attributed to Hiroshi Nikaido, nicknamed "the porinologist."[11]
According toTCDB, there are five evolutionarily independentsuperfamilies of porins. Porin superfamily I includes 47 families of porins with a range of numbers oftrans-membrane β-strands (β-TMS). These include the GBP, SP and RPP porin families. While PSF I includes 47 families, PSF II-V each contain only 2 families. While PSF I derives members fromgram-negative bacteria primarily one family of eukaryotic mitochondrial porins, PSF II and V porins are derived fromActinomycetota. PSF III and V are derived from eukaryotic organelle.[12][13]
1.B.1 - TheGeneral bacterial porin family
1.B.2 - The Chlamydial Porin (CP) Family
1.B.3 - TheSugar porin (SP) Family
1.B.4 - TheBrucella-Rhizobium porin (BRP) Family
1.B.5 - ThePseudomonas OprP Porin (POP) Family
1.B.6 -OmpA-OmpF porin (OOP) family
1.B.7Rhodobacter PorCa porin (RPP) family
1.B.8Mitochondrial and plastid porin (MPP) family
1.B.9FadL outer membrane protein (FadL) family
1.B.10Nucleoside-specific channel-forming outer membrane porin (Tsx) family
1.B.11 Outer membrane fimbrial usher porin (FUP) family
1.B.12Autotransporter-1 (AT-1) family
1.B.13Alginate export porin (AEP) family
1.B.14Outer membrane receptor (OMR) family
1.B.15 Raffinose porin (RafY) family
1.B.16 Short chain amide and urea porin (SAP) family
1.B.17Outer membrane factor (OMF) family
1.B.18Outer membrane auxiliary (OMA) protein family
1.B.19 Glucose-selective OprB porin (OprB) family
1.B.20 Two-partner secretion (TPS) family
1.B.21OmpG porin (OmpG) family
1.B.22 Outer bacterial membrane secretin (secretin) family
1.B.23 Cyanobacterial porin (CBP) family
1.B.24Mycobacterial porin
1.B.25Outer membrane porin (Opr) family
1.B.26 Cyclodextrin porin (CDP) family
1.B.31Campylobacter jejuni major outer membrane porin (MomP) family
1.B.32 Fusobacterial outer membrane porin (FomP) family
1.B.33 Outer membrane protein insertion porin (Bam complex) (OmpIP) family
1.B.34Corynebacterial porins
1.B.35Oligogalacturonate-specific porin (KdgM) family
1.B.39Bacterial porin, OmpW (OmpW) family
1.B.42 - The Outer Membrane Lipopolysaccharide Export Porin (LPS-EP) Family
1.B.43 - TheCoxiella Porin P1 (CPP1) Family
1.B.44 - The Probable Protein TranslocatingPorphyromonas gingivalis Porin (PorT) Family
1.B.49 - TheAnaplasma P44 (A-P44) Porin Family
1.B.54 -Intimin/Invasin (Int/Inv) orAutotransporter-3 family
1.B.55 - The Poly Acetyl Glucosamine Porin (PgaA) Family
1.B.57 - The Legionella Major-Outer Membrane Protein (LM-OMP) Family
1.B.60 - The Omp50 Porin (Omp50 Porin) Family
1.B.61 - The Delta-Proteobacterial Porin (Delta-Porin) Family
1.B.62 - The Putative Bacterial Porin (PBP) Family
1.B.66 - The Putative Beta-Barrel Porin-2 (BBP2) Family
1.B.67 - The Putative Beta Barrel Porin-4 (BBP4) Family
1.B.68 - The Putative Beta Barrel Porin-5 (BBP5) Superfamily
1.B.70 - The Outer Membrane Channel (OMC) Family
1.B.71 - The Proteobacterial/Verrucomicrobial Porin (PVP) Family
1.B.72 - The Protochlamydial Outer Membrane Porin (PomS/T) Family
1.B.73 - The Capsule Biogenesis/Assembly (CBA) Family
1.B.78 - The DUF3374 Electron Transport-associated Porin (ETPorin) Family
1.B.24 -Mycobacterial porin
1.B.58 - Nocardial Hetero-oligomeric Cell Wall Channel (NfpA/B) Family
1.B.28 - The Plastid Outer Envelope Porin of 24 kDa (OEP24) Family
1.B.47 - The Plastid Outer Envelope Porin of 37 kDa (OEP37) Family
This superfamily includes protein that comprise pores in multicomponent protein translocases as follows: 3.A.8 - [Tim17 (P39515) Tim22 (Q12328) Tim23 (P32897)]; 1.B.69 - [PXMP4 (Q9Y6I8) PMP24 (A2R8R0)]; 3.D.9 - [NDH 21.3 kDa component (P25710)]
1.B.30 - The Plastid Outer Envelope Porin of 16 kDa (OEP16) Family
1.B.69 - The Peroxysomal Membrane Porin 4 (PxMP4) Family
3.A.8 - TheMitochondrial Protein Translocase (MPT) Family
1.B.34 - The Corynebacterial Porin A (PorA) Family1.B.59 - The Outer Membrane Porin, PorH (PorH) Family