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]
Function
The MATE proteins in
bacteria,
archaea and
eukaryotes function as fundamental transporters of metabolic and xenobiotic organic cations.[2][3]
Structure
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]
Discovery
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]
^
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.
PMID19100867.
^
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.