| Literature DB >> 9546221 |
R A Grant1, D J Filman, S E Finkel, R Kolter, J M Hogle.
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.Entities:
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Year: 1998 PMID： 9546221 DOI： 10.1038/nsb0498-294
Source DB: PubMed Journal: Nat Struct Biol ISSN： 1072-8368