Abstract
Members of the major facilitator superfamily (MFS) of transport proteins are essential for the movement of a wide range of substrates across biomembranes. As this transport requires a series of conformational changes, structures of MFS transporters captured in different conformational states are needed to decipher the transport mechanism. Recently, a large number of MFS transporter structures have been determined, which has provided us with an unprecedented opportunity to understand general aspects of the transport mechanism. We propose an updated model for the conformational cycle of MFS transporters, the 'clamp-and-switch model', and discuss the role of so-called 'gating residues' and the substrate in modulating these conformational changes.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Allosteric Regulation
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Animals
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Arabidopsis / genetics
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Arabidopsis / metabolism
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Autoimmune Diseases / genetics
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Autoimmune Diseases / metabolism*
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Autoimmune Diseases / pathology
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Bacteria / genetics
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Bacteria / metabolism
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Biological Transport
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Cardiovascular Diseases / genetics
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Cardiovascular Diseases / metabolism*
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Cardiovascular Diseases / pathology
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Crystallography, X-Ray
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Gene Expression
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Humans
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Membrane Transport Proteins / chemistry*
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Membrane Transport Proteins / genetics
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Membrane Transport Proteins / metabolism
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Membrane Transport Proteins / ultrastructure
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Models, Molecular*
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Neoplasms / genetics
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Neoplasms / metabolism*
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Neoplasms / pathology
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Neurodegenerative Diseases / genetics
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Neurodegenerative Diseases / metabolism*
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Neurodegenerative Diseases / pathology
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Protein Structure, Secondary
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Protein Structure, Tertiary
Substances
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Membrane Transport Proteins