Crystal structures of a nicotine MATE transporter provide insight into its mechanism of substrate transport. Issue 14 (16th June 2021)

• Record Type: Journal Article
• Authors: Tanaka, Yoshiki; Iwaki, Shigehiro; Sasaki, Akira; Tsukazaki, Tomoya
• Editors: Griesinger, Christian
• Is Part Of: FEBS letters. Volume 595:Issue 14(2021)
• Page Start: 1902
• Page End: 1913
• Publication Date: 2021-06-16
• Subjects: lipidic cubic phase -- membrane protein -- nicotine transport -- X‐ray crystallography; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1002/1873-3468.14136
• Languages: English
• ISSNs: 0014-5793

Abstract

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. Abstract :