Structural and functional diversity calls for a new classification of ABC transporters
Copyright policy )Structural and functional diversity calls for a new classification of ABC transporters
Members of the ATP‐binding cassette (ABC) transporter superfamily translocate a broad spectrum of chemically diverse substrates. While their eponymous ATP‐binding cassette in the nucleotide‐binding domains (NBDs) is highly conserved, their transmembrane domains (TMDs) forming the translocation pathway exhibit distinct folds and topologies, suggesting that during evolution the ancient motor domains were combined with different transmembrane mechanical systems to orchestrate a variety of cellular processes. In recent years, it has become increasingly evident that the distinct TMD folds are best suited to categorize the multitude of ABC transporters. We therefore propose a new ABC transporter classification that is based on structural homology in the TMDs.
- Institute of Science Tokyo Japan
- University of Alabama at Birmingham United States
- Kyoto University Japan
- Beijing National Laboratory for Molecular Sciences China (People's Republic of)
- Chinese Academy of Sciences, Institute of Zoology China (People's Republic of)
Protein Folding, Solute carrier family, ray crystallography, ATPases, PROTEIN, membrane proteins, FOS: Health sciences, phylogeny, Biochemistry, Gene, Transmembrane domain, Computational biology, BINDING CASSETTE TRANSPORTER, molecular machines, structural biology, CRYSTAL-STRUCTURE, ARCHITECTURE, Nutrition and Dietetics, Mechanisms and Applications of RNA Interference, ABC Transporters, Life Sciences, ATP-dependent Transporters, Homology modeling, SUPERFAMILY, [SDV] Life Sciences [q-bio], Homology (biology), ABC transporters, Oncology, sequence alignment, Sequence homology, Medicine, ddc:570, Receptor, 570, ddc:540, Nursing, Transporter, Article, Transmembrane protein, Protein Domains, Copper and Zinc in Health and Disease, Biochemistry, Genetics and Molecular Biology, Health Sciences, ATP-binding cassette transporter, Genetics, Peptide sequence, Molecular Biology, Biology, X-ray crystallography, Mechanisms of Multidrug Resistance in Cancer, primary active transporters, 540, cryo‐, EM, Enzyme, FOS: Biological sciences, X‐, cryo-EM, ATP-Binding Cassette Transporters, ddc: ddc:540, ddc: ddc:570
Protein Folding, Solute carrier family, ray crystallography, ATPases, PROTEIN, membrane proteins, FOS: Health sciences, phylogeny, Biochemistry, Gene, Transmembrane domain, Computational biology, BINDING CASSETTE TRANSPORTER, molecular machines, structural biology, CRYSTAL-STRUCTURE, ARCHITECTURE, Nutrition and Dietetics, Mechanisms and Applications of RNA Interference, ABC Transporters, Life Sciences, ATP-dependent Transporters, Homology modeling, SUPERFAMILY, [SDV] Life Sciences [q-bio], Homology (biology), ABC transporters, Oncology, sequence alignment, Sequence homology, Medicine, ddc:570, Receptor, 570, ddc:540, Nursing, Transporter, Article, Transmembrane protein, Protein Domains, Copper and Zinc in Health and Disease, Biochemistry, Genetics and Molecular Biology, Health Sciences, ATP-binding cassette transporter, Genetics, Peptide sequence, Molecular Biology, Biology, X-ray crystallography, Mechanisms of Multidrug Resistance in Cancer, primary active transporters, 540, cryo‐, EM, Enzyme, FOS: Biological sciences, X‐, cryo-EM, ATP-Binding Cassette Transporters, ddc: ddc:540, ddc: ddc:570
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