Crystal structures of a nicotine MATE transporter provide insight into its mechanism of substrate transport

Autor: Shigehiro Iwaki, Yoshiki Tanaka, Tomoya Tsukazaki, Akira Sasaki
Jazyk: angličtina
Rok vydání: 2021
Předmět:
Models
Molecular
Protein Conformation
alpha-Helical
Nicotiana tabacum
Gene Expression
Vacuole
Crystallography
X-Ray
Biochemistry
Plant Roots
Substrate Specificity
Structural Biology
membrane protein
Cloning
Molecular
Plant Proteins
0303 health sciences
biology
Chemistry
Vacuolar lumen
030302 biochemistry & molecular biology
Transmembrane protein
Recombinant Proteins
Membrane
nicotine transport
Protein Binding
Nicotine
Organic Cation Transport Proteins
Genetic Vectors
Biophysics
03 medical and health sciences
Plant Cells
Tobacco
Genetics
Protein Interaction Domains and Motifs
Amino Acid Sequence
Molecular Biology
030304 developmental biology
X-ray crystallography
Binding Sites
Sequence Homology
Amino Acid
Substrate (chemistry)
Transporter
Biological Transport
Cell Biology
Intracellular Membranes
biology.organism_classification
Membrane protein
Saccharomycetales
Vacuoles
lipidic cubic phase
Sequence Alignment
Zdroj: FEBS Letters. 595(14):1902-1913
ISSN: 1873-3468
Popis: 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.
Databáze: OpenAIRE
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