Multi-antimicrobial extrusion protein (MATE) also known as multidrug and toxin extrusionormultidrug and toxic compound extrusion is a family of proteins which function as drug/sodium or proton antiporters.[1][2][3]
Multi antimicrobial extrusion protein | |||||||||
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Identifiers | |||||||||
Symbol | MatE | ||||||||
Pfam | PF01554 | ||||||||
Pfam clan | CL0222 | ||||||||
InterPro | IPR002528 | ||||||||
TCDB | 2.A.66 | ||||||||
OPM superfamily | 220 | ||||||||
OPM protein | 3mkt | ||||||||
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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:
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