Abstract
The crystal structure of Dps, a DNA-binding protein from starved E. coli that protects DNA from oxidative damage, has been solved at 1.6 A resolution. The Dps monomer has essentially the same fold as ferritin, which forms a 24-mer with 432 symmetry, a hollow core and pores at the three-fold axes. Dps forms a dodecamer with 23 (tetrahedral) point group symmetry which also has a hollow core and pores at the three-folds. The structure suggests a novel DNA-binding motif and a mechanism for DNA protection based on the sequestration of Fe ions.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Bacterial Proteins / chemistry*
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Bacterial Proteins / metabolism*
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Binding Sites
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Crystallography, X-Ray
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DNA / chemistry*
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DNA / metabolism*
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DNA-Binding Proteins / chemistry*
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DNA-Binding Proteins / metabolism*
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Escherichia coli / physiology
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Ferritins / chemistry*
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Macromolecular Substances
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Models, Molecular
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Molecular Sequence Data
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Oxidative Stress
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Point Mutation
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Protein Conformation*
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Protein Folding
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Protein Structure, Secondary
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Sequence Alignment
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Sequence Homology, Amino Acid
Substances
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Bacterial Proteins
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DNA-Binding Proteins
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DPS protein, Bacteria
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Macromolecular Substances
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Recombinant Proteins
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DNA
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Ferritins