3MKU
Structure of a Cation-bound Multidrug and Toxin Compound Extrusion (MATE) transporter
Summary for 3MKU
| Entry DOI | 10.2210/pdb3mku/pdb |
| Related | 3MKT |
| Descriptor | Multi antimicrobial extrusion protein (Na(+)/drug antiporter) MATE-like MDR efflux pump, RUBIDIUM ION (2 entities in total) |
| Functional Keywords | mate, multidrug transporter, cation-bound, transport protein |
| Biological source | Vibrio cholerae |
| Total number of polymer chains | 2 |
| Total formula weight | 99693.20 |
| Authors | He, X.,Szewczyk, P.,Karyakin, A.,Evin, M.,Hong, W.-X.,Zhang, Q.,Chang, G. (deposition date: 2010-04-15, release date: 2010-09-29, Last modification date: 2024-02-21) |
| Primary citation | He, X.,Szewczyk, P.,Karyakin, A.,Evin, M.,Hong, W.X.,Zhang, Q.,Chang, G. Structure of a cation-bound multidrug and toxic compound extrusion transporter. Nature, 467:991-994, 2010 Cited by PubMed Abstract: Transporter proteins from the MATE (multidrug and toxic compound extrusion) family are vital in metabolite transport in plants, directly affecting crop yields worldwide. MATE transporters also mediate multiple-drug resistance (MDR) in bacteria and mammals, modulating the efficacy of many pharmaceutical drugs used in the treatment of a variety of diseases. MATE transporters couple substrate transport to electrochemical gradients and are the only remaining class of MDR transporters whose structure has not been determined. Here we report the X-ray structure of the MATE transporter NorM from Vibrio cholerae 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 MDR transporter. We also report a cation-binding site in close proximity to residues previously deemed critical for transport. This conformation probably represents a stage of the transport cycle with high affinity for monovalent cations and low affinity for substrates. PubMed: 20861838DOI: 10.1038/nature09408 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (4.2 Å) |
Structure validation
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