The Crystal Structure of Dps, a Ferritin Homolog That Binds and Protects DNA

Overview

Journal Nat Struct Biol

Specialty Cell Biology

Date 1998 Apr 18

PMID 9546221

Citations 180

Authors

R A Grant

D J Filman

S E Finkel

R Kolter

J M Hogle

Affiliations

Soon will be listed here.

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.

Citing Articles

Gene knockout studies of Dps protein reveals a novel role for DNA-binding protein in maintaining outer membrane permeability.

Pant I, Potnis A, Shashidhar R World J Microbiol Biotechnol. 2025; 41(2):70.

PMID: 39939516 PMC: 11821673. DOI: 10.1007/s11274-025-04269-y.

The Dps Protein Protects DNA in the Form of the Trimer.

Kovalenko V, Tereshkina K, Moiseenko A, Ryzhykau Y, Kuklin A, Tereshkin E Int J Mol Sci. 2025; 26(2).

PMID: 39859335 PMC: 11766142. DOI: 10.3390/ijms26020619.

A Brief History of Ferritin, an Ancient and Versatile Protein.

Arosio P, Cairo G, Bou-Abdallah F Int J Mol Sci. 2025; 26(1.

PMID: 39796064 PMC: 11719527. DOI: 10.3390/ijms26010206.

Self-Assembled Ferritin Nanoparticles for Delivery of Antigens and Development of Vaccines: From Structure and Property to Applications.

Cao S, Ma D, Ji S, Zhou M, Zhu S Molecules. 2024; 29(17).

PMID: 39275069 PMC: 11397193. DOI: 10.3390/molecules29174221.

Bioactive Molecules Delivery through Ferritin Nanoparticles: Sum Up of Current Loading Methods.

Lucignano R, Ferraro G Molecules. 2024; 29(17).

PMID: 39274893 PMC: 11396501. DOI: 10.3390/molecules29174045.