Abstract
Membrane transporter proteins are critical for cellular uptake and export of molecules, and are reported to function by a number of different molecular mechanisms. The new occluded state structure of the uracil transporter, UraA, from Escherichia coli, reveals that both coordinated movement of the two domains of a single protomer together with dimer formation are important for transport activity.
MeSH terms
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Biological Transport, Active / physiology
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Escherichia coli Proteins* / chemistry
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Escherichia coli Proteins* / genetics
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Escherichia coli Proteins* / metabolism
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Escherichia coli* / chemistry
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Escherichia coli* / genetics
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Escherichia coli* / metabolism
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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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Protein Domains
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Protein Multimerization*
Substances
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Escherichia coli Proteins
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Membrane Transport Proteins
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UraA protein, E coli