The crystal structure of Dps, a ferritin homolog that binds and protects DNA

The crystal structure of Dps, a DNA-binding protein from starved E. coli that protects DMA from oxidative damage, has been solved at 1.6 Å 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. Dp...

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Veröffentlicht in:	Nature Structural Biology 1998-04, Vol.5 (4), p.294-303
Hauptverfasser:	Grant, R.A., Filman, D.J., Finkel, S.E., Kolter, R., Hogle, J.M.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Bacterial Proteins - chemistry Bacterial Proteins - metabolism Binding Sites Biochemistry Biological Microscopy Biomedical and Life Sciences Crystallography, X-Ray DNA - chemistry DNA - metabolism DNA-Binding Proteins - chemistry DNA-Binding Proteins - metabolism Escherichia coli Escherichia coli - physiology Ferritins - chemistry Life Sciences Macromolecular Substances Membrane Biology Models, Molecular Molecular Sequence Data Oxidative Stress Point Mutation Protein Conformation Protein Folding Protein Structure Protein Structure, Secondary Recombinant Proteins - chemistry Recombinant Proteins - metabolism Sequence Alignment Sequence Homology, Amino Acid
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