Abstract
Building a three-dimensional model of the sucrose permease of Escherichia coli (CscB) with the X-ray crystal structure lactose permease (LacY) as template reveals a similar overall fold for CscB. Moreover, despite only 28% sequence identity and a marked difference in substrate specificity, the structural organization of the residues involved in sugar-binding and H(+) translocation is conserved in CscB. Functional analyses of mutants in the homologous key residues provide strong evidence that they play a similar critical role in the mechanisms of CscB and LacY.
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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Amino Acid Sequence
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Binding Sites / genetics
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Carbohydrate Metabolism
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Conserved Sequence
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Escherichia coli / genetics
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Escherichia coli / metabolism*
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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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Genes, Bacterial
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Hydrogen / metabolism
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Kinetics
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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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Models, Molecular
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Monosaccharide Transport Proteins / chemistry*
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Monosaccharide Transport Proteins / genetics
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Monosaccharide Transport Proteins / metabolism*
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Mutagenesis, Site-Directed
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Symporters / chemistry*
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Symporters / genetics
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Symporters / metabolism*
Substances
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Escherichia coli Proteins
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LacY protein, E coli
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Membrane Transport Proteins
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Monosaccharide Transport Proteins
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Recombinant Proteins
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Symporters
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cscB protein, E coli
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Hydrogen