The crystal structure of Dps, a ferritin homolog that binds and protects DNA
RA Grant, DJ Filman, SE Finkel, R Kolter… - Nature structural …, 1998 - nature.com
RA Grant, DJ Filman, SE Finkel, R Kolter, JM Hogle
Nature structural biology, 1998•nature.comThe 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. 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 …
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. 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 …
Abstract
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. 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.
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