Structure of the periplasmic adaptor protein from a major facilitator superfamily (MFS) multidrug efflux pump.
FEBS Lett
; 588(17): 3147-53, 2014 Aug 25.
Article
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| MEDLINE
| ID: mdl-24996185
Periplasmic adaptor proteins are key components of bacterial tripartite efflux pumps. The 2.85 Å resolution structure of an MFS (major facilitator superfamily) pump adaptor, Aquifex aeolicus EmrA, shows linearly arranged α-helical coiled-coil, lipoyl, and ß-barrel domains, but lacks the fourth membrane-proximal domain shown in other pumps to interact with the inner membrane transporter. The adaptor α-hairpin, which binds outer membrane TolC, is exceptionally long at 127 Å, and the ß-barrel contains a conserved disordered loop. The structure extends the view of adaptors as flexible, modular components that mediate diverse pump assembly, and suggests that in MFS tripartite pumps a hexamer of adaptors could provide a periplasmic seal.
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1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Proteínas de Transporte de Membrana
/
Proteínas Bacterianas
Idioma:
En
Revista:
FEBS Lett
Año:
2014
Tipo del documento:
Article