Multi-antimicrobialextrusion protein (MATE) also known asmultidrug and toxin extrusion ormultidrug and toxic compound extrusion is a family ofproteins which function as drug/sodium or protonantiporters.[1][2][3]
These proteins are predicted to have 12alpha-helicaltransmembrane regions, some of the animal proteins may have an additionalC-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 multidrugeffluxtransporterNorM fromV. parahaemolyticus which mediates resistance to multiple antimicrobial agents (norfloxacin,kanamycin,ethidium bromide etc.) and its homologue fromE. coli were identified in 1998.[6] NorM seems to function as drug/sodiumantiporter which is the first example of Na+-coupled multidrugefflux transporter discovered.[7] NorM is a prototype of a newtransporter family and Brownet 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]
^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.PMID16996621.
