Multi-antimicrobial extrusion protein

From Wikipedia, the free encyclopedia
Jump to navigation Jump to search
Multi antimicrobial extrusion protein
Pfam clanCL0222
OPM superfamily220
OPM protein3mkt

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[edit]


  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. doi:10.1046/j.1365-2958.1999.01162.x. PMID 9987140.
  2. ^ 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.
  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. doi:10.1016/ PMID 16996621.
  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. doi:10.1046/j.1432-1033.2003.03418.x. PMID 12603313.
  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. doi:10.1038/nature09408. PMC 3152480. PMID 20861838.
  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. doi:10.1128/AAC.42.7.1778. 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. doi:10.1128/JB.182.23.6694-6697.2000. PMC 111412. PMID 11073914.
  8. ^ van Veen HW (2010). "Structural biology: Last of the multidrug transporters". Nature. 467 (7318): 926–7. doi:10.1038/467926a. PMID 20962836.
This article incorporates text from the public domain Pfam and InterPro: IPR002528