ArticleProceedings of the National Academy of Sciences of the United States of America2013
Evolutionary mix-and-match with MFS transporters II.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- A Key Metabolic Protein in Active Mycobacterium tuberculosis: Insights into Carbon, Nitrogen, and Sulfur Metabolism.Advances in experimental medicine and biology · 2026Review
- Genetically encoded biosensor enabled mining, characterisation and engineering of aromatic acid MFS transporters.Journal of biological engineering · 2025Article
- Ins and Outs of Rocker Switch Mechanism in Major Facilitator Superfamily of Transporters.Membranes · 2023Review
- Spontaneous Suppressors against Debilitating Transmembrane Mutants ofJournal of fungi (Basel, Switzerland) · 2022Article
- Variations in exons 11 and 12 of the multi-pest resistance wheat geneFrontiers in plant science · 2022Article
- Molecular characterization of a novel strain ofFrontiers in plant science · 2022Article
- Structures and General Transport Mechanisms by the Major Facilitator Superfamily (MFS).Chemical reviews · 2021Article
- Insight into determinants of substrate binding and transport in a multidrug efflux protein.Scientific reports · 2016Article
- Experimentally optimized threading structures of the proton-coupled folate transporter.FEBS open bio · 2016Article
- A Numbering System for MFS Transporter Proteins.Frontiers in molecular biosciences · 2016Article
- Article
- A Mycobacterium avium subsp. paratuberculosis Predicted Serine Protease Is Associated with Acid Stress and Intraphagosomal Survival.Frontiers in cellular and infection microbiology · 2016Article
- Identification and functional characterization of novel xylose transporters from the cell factories Aspergillus niger and Trichoderma reesei.Biotechnology for biofuels · 2016Article
- Crystal Structures of the Extracellular Domain from PepT1 and PepT2 Provide Novel Insights into Mammalian Peptide Transport.Structure (London, England : 1993) · 2015Article
- Computation and Functional Studies Provide a Model for the Structure of the Zinc Transporter hZIP4.The Journal of biological chemistry · 2015Article
- Molecular insights into proton coupled peptide transport in the PTR family of oligopeptide transporters.Biochimica et biophysica acta · 2015Review
- A chemiosmotic mechanism of symport.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Major Facilitator Superfamily (MFS) evolved without 3-transmembrane segment unit rearrangements.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Functional architecture of MFS D-glucose transporters.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Structure of sugar-bound LacY.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
One fundamentally important problem for understanding the mechanism of coupling between substrate and H(+) translocation with secondary active transport proteins is the identification and physical localization of residues involved in substrate and H(+) binding. This information is exceptionally difficult to obtain with the Major Facilitator Superfamily (MFS) because of the broad sequence diversity of the members. The MFS is the largest and most diverse group of transporters, many of which are clinically important, and includes members from all kingdoms of life. A wide range of substrates is transported, in many instances against a concentration gradient by transduction of the energy stored in an H(+) electrochemical gradient using symport mechanisms, which are discussed herein. Crystallographic structures of MFS members indicate that a deep central hydrophilic cavity surrounded by 12 mostly irregular transmembrane helices represents a common structural feature. An inverted triple-helix structural symmetry motif within the N- and C-terminal six-helix bundles suggests that the proteins may have arisen by intragenic multiplication. In the work presented here, the triple-helix motifs are aligned in combinatorial fashion so as to detect functionally homologous positions with known atomic structures of MFS members. Substrate and H(+)-binding sites in symporters that transport substrates, ranging from simple ions like phosphate to more complex peptides or disaccharides, are found to be in similar locations. It also appears likely that there is a homologous ordered kinetic mechanism for the H(+)-coupled MFS symporters.
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