4TKO
Structure of the periplasmic adaptor protein EmrA
Summary for 4TKO
| Entry DOI | 10.2210/pdb4tko/pdb |
| Descriptor | EmrA, MAGNESIUM ION, ISOPROPYL ALCOHOL, ... (4 entities in total) |
| Functional Keywords | mfs, multidrug resistance, periplasmic adaptor, membrane protein |
| Biological source | Aquifex aeolicus |
| Total number of polymer chains | 1 |
| Total formula weight | 41466.82 |
| Authors | Hinchliffe, P.,Greene, N.P.,Paterson, N.G.,Crow, A.,Hughes, C.,Koronakis, V. (deposition date: 2014-05-27, release date: 2014-07-09, Last modification date: 2023-12-27) |
| Primary citation | Hinchliffe, P.,Greene, N.P.,Paterson, N.G.,Crow, A.,Hughes, C.,Koronakis, V. Structure of the periplasmic adaptor protein from a major facilitator superfamily (MFS) multidrug efflux pump. Febs Lett., 588:3147-3153, 2014 Cited by PubMed Abstract: 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 β-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 β-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. PubMed: 24996185DOI: 10.1016/j.febslet.2014.06.055 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.85 Å) |
Structure validation
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