Multi-antimicrobial extrusion protein (MATE) also known as multidrug and toxin extrusion or multidrug and toxic compound extrusion is a family of proteins which function as drug/sodium or proton antiporters.[1][2][3]
The MATE proteins in bacteria, archaea and eukaryotes function as fundamental transporters of metabolic and xenobiotic organic cations.[2][3]
Structureedit
These proteins are predicted to have 12 alpha-helicaltransmembrane regions, some of the animal proteins may have an additional C-terminal helix.[4] The X-ray structure of the NorM was determined to 3.65 Å, revealing an outward-facing conformation with two portals open to the outer leaflet of the membrane and a unique topology of the predicted 12 transmembrane helices distinct from any other known multidrug resistance transporter.[5]
Discoveryedit
The multidrug effluxtransporterNorM from V. parahaemolyticus which mediates resistance to multiple antimicrobial agents (norfloxacin, kanamycin, ethidium bromide etc.) and its homologue from E. coli were identified in 1998.[6] NorM seems to function as drug/sodium antiporter which is the first example of Na+-coupled multidrug efflux transporter discovered.[7] NorM is a prototype of a new transporter family and Brown et al. named it the multidrug and toxic compound extrusion family.[1] NorM is nicknamed "Last of the multidrug transporters" because it is the last multidrug transporter discovered functionally as well as structurally.[8]
^ abBrown MH, Paulsen IT, Skurray RA (January 1999). "The multidrug efflux protein NorM is a prototype of a new family of transporters". Mol. Microbiol. 31 (1): 394–5. doi:10.1046/j.1365-2958.1999.01162.x. PMID 9987140. S2CID 39261040.
^ abKuroda T, Tsuchiya T (December 2008). "Multidrug efflux transporters in the MATE family". Biochim. Biophys. Acta. 1794 (5): 763–8. doi:10.1016/j.bbapap.2008.11.012. PMID 19100867.
^ abOmote H; et al. (2006). "The MATE proteins as fundamental transporters of metabolic and xenobiotic organic cations". Trends in Pharmacological Sciences. 27 (11): 587–93. doi:10.1016/j.tips.2006.09.001. PMID 16996621.
^Hvorup RN, Winnen B, Chang AB, Jiang Y, Zhou XF, Saier MH (March 2003). "The multidrug/oligosaccharidyl-lipid/polysaccharide (MOP) exporter superfamily". Eur. J. Biochem. 270 (5): 799–813. doi:10.1046/j.1432-1033.2003.03418.x. PMID 12603313.
^He X, Szewczyk P, Karykin A, Hong WX, Zhang Q, Chang G (2010). "Structure of a Cation-bound Multidrug and Toxic Compound Extrusion Transporter". Nature. 467 (7318): 991–994. Bibcode:2010Natur.467..991H. doi:10.1038/nature09408. PMC3152480. PMID 20861838.
^Morita Y, Kodama K, Shiota S, Mine T, Kataoka A, Mizushima T, Tsuchiya T (July 1998). "NorM, a Putative Multidrug Efflux Protein, of Vibrio parahaemolyticus and Its Homolog in Escherichia coli". Antimicrob. Agents Chemother. 42 (7): 1778–82. doi:10.1128/AAC.42.7.1778. PMC105682. PMID 9661020.
^Morita Y, Kataoka A, Shiota S, Mizushima T, Tsuchiya T (December 2000). "NorM of Vibrio parahaemolyticus Is an Na+-Driven Multidrug Efflux Pump". J. Bacteriol. 182 (23): 6694–7. doi:10.1128/JB.182.23.6694-6697.2000. PMC111412. PMID 11073914.
^van Veen HW (2010). "Structural biology: Last of the multidrug transporters". Nature. 467 (7318): 926–7. Bibcode:2010Natur.467..926V. doi:10.1038/467926a. PMID 20962836. S2CID 4338964.
This article incorporates text from the public domain Pfam and InterPro: IPR002528
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multi, antimicrobial, extrusion, protein, other, uses, mate, mate, also, known, multidrug, toxin, extrusion, multidrug, toxic, compound, extrusion, family, proteins, which, function, drug, sodium, proton, antiporters, multi, antimicrobial, extrusion, proteinid. For other uses see Mate Multi antimicrobial extrusion protein MATE also known as multidrug and toxin extrusion or multidrug and toxic compound extrusion is a family of proteins which function as drug sodium or proton antiporters 1 2 3 Multi antimicrobial extrusion proteinIdentifiersSymbolMatEPfamPF01554Pfam clanCL0222InterProIPR002528TCDB2 A 66OPM superfamily220OPM protein3mktAvailable protein structures Pfam structures ECOD PDBRCSB PDB PDBe PDBjPDBsumstructure summary Contents 1 Function 2 Structure 3 Discovery 4 Genes 5 See also 6 ReferencesFunction editThe MATE proteins in bacteria archaea and eukaryotes function as fundamental transporters of metabolic and xenobiotic organic cations 2 3 Structure editThese proteins are predicted to have 12 alpha helical transmembrane regions some of the animal proteins may have an additional C terminal helix 4 The X ray structure of the NorM was determined to 3 65 A revealing an outward facing conformation with two portals open to the outer leaflet of the membrane and a unique topology of the predicted 12 transmembrane helices distinct from any other known multidrug resistance transporter 5 Discovery editThe multidrug efflux transporter NorM from V parahaemolyticus which mediates resistance to multiple antimicrobial agents norfloxacin kanamycin ethidium bromide etc and its homologue from E coli were identified in 1998 6 NorM seems to function as drug sodium antiporter which is the first example of Na coupled multidrug efflux transporter discovered 7 NorM is a prototype of a new transporter family and Brown et al named it the multidrug and toxic compound extrusion family 1 NorM is nicknamed Last of the multidrug transporters because it is the last multidrug transporter discovered functionally as well as structurally 8 Genes editThe following human genes encode MATE proteins SLC47A1 SLC47A2See also editSolute carrier family Resistance Nodulation Cell Division Superfamily RND References edit a b Brown MH Paulsen IT Skurray RA January 1999 The multidrug efflux protein NorM is a prototype of a new family of transporters Mol Microbiol 31 1 394 5 doi 10 1046 j 1365 2958 1999 01162 x PMID 9987140 S2CID 39261040 a b Kuroda T Tsuchiya T December 2008 Multidrug efflux transporters in the MATE family Biochim Biophys Acta 1794 5 763 8 doi 10 1016 j bbapap 2008 11 012 PMID 19100867 a b Omote H et al 2006 The MATE proteins as fundamental transporters of metabolic and xenobiotic organic cations Trends in Pharmacological Sciences 27 11 587 93 doi 10 1016 j tips 2006 09 001 PMID 16996621 Hvorup RN Winnen B Chang AB Jiang Y Zhou XF Saier MH March 2003 The multidrug oligosaccharidyl lipid polysaccharide MOP exporter superfamily Eur J Biochem 270 5 799 813 doi 10 1046 j 1432 1033 2003 03418 x PMID 12603313 He X Szewczyk P Karykin A Hong WX Zhang Q Chang G 2010 Structure of a Cation bound Multidrug and Toxic Compound Extrusion Transporter Nature 467 7318 991 994 Bibcode 2010Natur 467 991H doi 10 1038 nature09408 PMC 3152480 PMID 20861838 Morita Y Kodama K Shiota S Mine T Kataoka A Mizushima T Tsuchiya T July 1998 NorM a Putative Multidrug Efflux Protein of Vibrio parahaemolyticus and Its Homolog in Escherichia coli Antimicrob Agents Chemother 42 7 1778 82 doi 10 1128 AAC 42 7 1778 PMC 105682 PMID 9661020 Morita Y Kataoka A Shiota S Mizushima T Tsuchiya T December 2000 NorM of Vibrio parahaemolyticus Is an Na Driven Multidrug Efflux Pump J Bacteriol 182 23 6694 7 doi 10 1128 JB 182 23 6694 6697 2000 PMC 111412 PMID 11073914 van Veen HW 2010 Structural biology Last of the multidrug transporters Nature 467 7318 926 7 Bibcode 2010Natur 467 926V doi 10 1038 467926a PMID 20962836 S2CID 4338964 This article incorporates text from the public domain Pfam and InterPro IPR002528 nbsp This membrane protein related article is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title Multi antimicrobial extrusion protein amp oldid 997763509, wikipedia, wiki, book, books, library,
