Template:STRUCTURE 1dps

File:1dps.jpg

THE CRYSTAL STRUCTURE OF DPS, A FERRITIN HOMOLOG THAT BINDS AND PROTECTS DNA


OverviewOverview

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.

About this StructureAbout this Structure

1DPS is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

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 Page seeded by OCA on Fri May 2 14:07:46 2008

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