Open Access Articles- Top Results for Multi-antimicrobial extrusion protein

Multi-antimicrobial extrusion protein

Multi-antimicrobial extrusion protein
Symbol MatE
Pfam PF01554
Pfam clan CL0222
InterPro IPR002528
TCDB 2.A.66
OPM superfamily 249
OPM protein 3mkt
For other uses, see [[Mate (disambiguation)#REDIRECTmw:Help:Magic words#Other
This page is a soft redirect.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]


The MATE proteins in bacteria, archaea and eukaryotes function as fundamental transporters of metabolic and xenobiotic organic cations.[2][3]


These 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 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]


The 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]


The following human genes encode MATE proteins:

See also


  1. ^ 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. PMID 9987140. doi:10.1046/j.1365-2958.1999.01162.x. 
  2. ^ a b Kuroda T, Tsuchiya T (December 2008). "Multidrug efflux transporters in the MATE family". Biochim. Biophys. Acta 1794 (5): 763–8. PMID 19100867. doi:10.1016/j.bbapap.2008.11.012. 
  3. ^ 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. PMID 16996621. doi:10.1016/ 
  4. ^ 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. PMID 12603313. doi:10.1046/j.1432-1033.2003.03418.x. 
  5. ^ 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. PMC 3152480. PMID 20861838. doi:10.1038/nature09408. 
  6. ^ 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. PMC 105682. PMID 9661020. 
  7. ^ 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. PMC 111412. PMID 11073914. doi:10.1128/JB.182.23.6694-6697.2000. 
  8. ^ van Veen HW (2010). "Structural biology: Last of the multidrug transporters". Nature 467 (7318): 926–7. PMID 20962836. doi:10.1038/467926a. 

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