Multidrug and toxin extrusion protein 1: Difference between revisions
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== Discovery == |
== Discovery == |
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The multidrug [[efflux]] [[transporter]] '''NorM''' from ''[[Vibrio parahaemolyticus|V. parahaemolyticus]]'' which mediates resistance to multiple antimicrobial agents ([[norfloxacin]], [[kanamycin]], [[ethidium bromide]] etc.) and its homologue from ''[[Escherichia coli|E. coli]]'' were identified in 1998, which is the first of Solute carrier family 47 member.<ref name="pmid9661020"/> NorM seems to function as drug/sodium [[antiporter]] which is the first example of Na<sup>+</sup>-coupled multidrug [[efflux]] transporter.<ref name="pmid11073914">{{cite journal | author = Morita Y, Kataoka A, Shiota S, Mizushima T, Tsuchiya T | title = NorM of vibrio parahaemolyticus is an Na(+)-driven multidrug efflux pump | journal = J. Bacteriol. | volume = 182 | issue = 23 | pages = 6694–7 | year = 2000 | month = December | pmid = 11073914 | pmc = 111412 | doi = 10.1128/JB.182.23.6694-6697.2000| url = | issn = }}</ref> NorM is a prototype of a new [[transporter]] family and Brown ''et al.''. named it the multidrug and toxic compound extrusion family.<ref name="pmid9987140"/> The X-ray structure of the transporter 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.<ref name="pmid20861838">{{cite journal | author = He X, Szewczyk P, Karykin A, Hong WX, Zhang Q, Chang G | title = Structure of a cation-bound multidrug and toxic compound extrusion transporter | journal = Nature | volume = 467| issue = 7318| pages = 991–4| year = 2010 | month = | pmid = 20861838 | doi = 10.1038/nature09408 | pmc=3152480}}</ref> |
The multidrug [[efflux (microbiology)|efflux]] [[Membrane transport protein|transporter]] '''NorM''' from ''[[Vibrio parahaemolyticus|V. parahaemolyticus]]'' which mediates resistance to multiple antimicrobial agents ([[norfloxacin]], [[kanamycin]], [[ethidium bromide]] etc.) and its homologue from ''[[Escherichia coli|E. coli]]'' were identified in 1998, which is the first of Solute carrier family 47 member.<ref name="pmid9661020"/> NorM seems to function as drug/sodium [[antiporter]] which is the first example of Na<sup>+</sup>-coupled multidrug [[efflux (microbiology)|efflux]] transporter.<ref name="pmid11073914">{{cite journal | author = Morita Y, Kataoka A, Shiota S, Mizushima T, Tsuchiya T | title = NorM of vibrio parahaemolyticus is an Na(+)-driven multidrug efflux pump | journal = J. Bacteriol. | volume = 182 | issue = 23 | pages = 6694–7 | year = 2000 | month = December | pmid = 11073914 | pmc = 111412 | doi = 10.1128/JB.182.23.6694-6697.2000| url = | issn = }}</ref> NorM is a prototype of a new [[Membrane transport protein|transporter]] family and Brown ''et al.''. named it the multidrug and toxic compound extrusion family.<ref name="pmid9987140"/> The X-ray structure of the transporter 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.<ref name="pmid20861838">{{cite journal | author = He X, Szewczyk P, Karykin A, Hong WX, Zhang Q, Chang G | title = Structure of a cation-bound multidrug and toxic compound extrusion transporter | journal = Nature | volume = 467| issue = 7318| pages = 991–4| year = 2010 | month = | pmid = 20861838 | doi = 10.1038/nature09408 | pmc=3152480}}</ref> |
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== See also == |
== See also == |
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Revision as of 00:28, 18 January 2013
Template:PBB Multidrug and toxin extrusion protein 1 (MATE1), also known as solute carrier family 47, member 1, is a protein that in humans is encoded by the SLC47A1 gene.[1][2] SLC47A1 belongs to the MATE (multidrug and toxic compound extrusion) family of transporters that are found in bacteria, archaea and eukaryotes.[3][4]
Gene
The SLC47A1 gene is located within the Smith-Magenis syndrome region on chromosome 17.[1]
Function
SLC47A1 is a member of the MATE family of transporters that excrete endogenous and exogenous toxic electrolytes through urine and bile.[2]
Discovery
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, which is the first of Solute carrier family 47 member.[3] NorM seems to function as drug/sodium antiporter which is the first example of Na+-coupled multidrug efflux transporter.[5] NorM is a prototype of a new transporter family and Brown et al.. named it the multidrug and toxic compound extrusion family.[4] The X-ray structure of the transporter 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.[6]
See also
- MATE (Multi antimicrobial extrusion protein or multidrug and toxic compound extrusion protein)
References
- ^ a b "Entrez Gene: FLJ10847 hypothetical protein FLJ10847".
- ^ a b Otsuka M, Matsumoto T, Morimoto R, Arioka S, Omote H, Moriyama Y (2005). "A human transporter protein that mediates the final excretion step for toxic organic cations". Proc. Natl. Acad. Sci. U.S.A. 102 (50): 17923–8. doi:10.1073/pnas.0506483102. PMC 1312386. PMID 16330770.
{{cite journal}}: Unknown parameter|month=ignored (help)CS1 maint: multiple names: authors list (link) - ^ a b Morita Y, Kodama K, Shiota S, Mine T, Kataoka A, Mizushima T, Tsuchiya T (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.
{{cite journal}}: Unknown parameter|month=ignored (help)CS1 maint: multiple names: authors list (link) - ^ a b Brown MH, Paulsen IT, Skurray RA (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.
{{cite journal}}: Unknown parameter|month=ignored (help)CS1 maint: multiple names: authors list (link) - ^ Morita Y, Kataoka A, Shiota S, Mizushima T, Tsuchiya T (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.
{{cite journal}}: Unknown parameter|month=ignored (help)CS1 maint: multiple names: authors list (link) - ^ 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): 991–4. doi:10.1038/nature09408. PMC 3152480. PMID 20861838.
{{cite journal}}: Cite has empty unknown parameter:|month=(help)CS1 maint: multiple names: authors list (link)
Further reading
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