Structural highlights
Evolutionary Conservation
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Publication Abstract from PubMed
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.
The crystal structure of Dps, a ferritin homolog that binds and protects DNA.,Grant RA, Filman DJ, Finkel SE, Kolter R, Hogle JM Nat Struct Biol. 1998 Apr;5(4):294-303. PMID:9546221[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Grant RA, Filman DJ, Finkel SE, Kolter R, Hogle JM. The crystal structure of Dps, a ferritin homolog that binds and protects DNA. Nat Struct Biol. 1998 Apr;5(4):294-303. PMID:9546221
