7DQK
A nicotine MATE transporter, Nicotiana tabacum MATE2 (NtMATE2)
Summary for 7DQK
| Entry DOI | 10.2210/pdb7dqk/pdb |
| Descriptor | Protein DETOXIFICATION, DI(HYDROXYETHYL)ETHER, (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate, ... (6 entities in total) |
| Functional Keywords | multidrug efflux transporter, transport protein |
| Biological source | Nicotiana tabacum (Common tobacco) |
| Total number of polymer chains | 2 |
| Total formula weight | 111846.09 |
| Authors | Tanaka, Y.,Tsukazaki, T.,Sasaki, A.,Iwaki, S. (deposition date: 2020-12-24, release date: 2021-06-09, Last modification date: 2023-11-29) |
| Primary citation | Tanaka, Y.,Iwaki, S.,Sasaki, A.,Tsukazaki, T. Crystal structures of a nicotine MATE transporter provide insight into its mechanism of substrate transport. Febs Lett., 595:1902-1913, 2021 Cited by PubMed Abstract: A transporter of the multidrug and toxic compound extrusion (MATE) family, Nicotiana tabacum MATE2 (NtMATE2), is located in the vacuole membrane of the tobacco plant root and is involved in the transportation of nicotine, a secondary or specialized metabolic compound in Solanaceae. Here, we report the crystal structures of NtMATE2 in its outward-facing forms. The overall structure has a bilobate V-shape with pseudo-symmetrical assembly of the N- and C-lobes. In one crystal structure, the C-lobe cavity of NtMATE2 interacts with an unidentified molecule that may partially mimic a substrate. In addition, NtMATE2-specific conformational transitions imply that an unprecedented movement of the transmembrane α-helix 7 is related to the release of the substrate into the vacuolar lumen. PubMed: 34050946DOI: 10.1002/1873-3468.14136 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.5 Å) |
Structure validation
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