5XJJ
Crystal structure of a MATE family protein
Summary for 5XJJ
| Entry DOI | 10.2210/pdb5xjj/pdb |
| Related | 5YCK |
| Descriptor | multi drug efflux transporter, (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate (3 entities in total) |
| Functional Keywords | membrane protein, multidrug resistance, transporter, transport protein |
| Biological source | Camelina sativa |
| Total number of polymer chains | 1 |
| Total formula weight | 49999.34 |
| Authors | Tanaka, Y.,Tsukazaki, T.,Iwaki, S. (deposition date: 2017-05-02, release date: 2017-09-20, Last modification date: 2023-11-22) |
| Primary citation | Tanaka, Y.,Iwaki, S.,Tsukazaki, T. Crystal Structure of a Plant Multidrug and Toxic Compound Extrusion Family Protein Structure, 25:1455-1460.e2, 2017 Cited by PubMed Abstract: The multidrug and toxic compound extrusion (MATE) family of proteins consists of transporters responsible for multidrug resistance in prokaryotes. In plants, a number of MATE proteins were identified by recent genomic and functional studies, which imply that the proteins have substrate-specific transport functions instead of multidrug extrusion. The three-dimensional structure of eukaryotic MATE proteins, including those of plants, has not been reported, preventing a better understanding of the molecular mechanism of these proteins. Here, we describe the crystal structure of a MATE protein from the plant Camelina sativa at 2.9 Å resolution. Two sets of six transmembrane α helices, assembled pseudo-symmetrically, possess a negatively charged internal pocket with an outward-facing shape. The crystal structure provides insight into the diversity of plant MATE proteins and their substrate recognition and transport through the membrane. PubMed: 28877507DOI: 10.1016/j.str.2017.07.009 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
Download full validation report
