The crystal structure of Dps, a ferritin homolog that binds and protects DNA

被引：433

作者：

Grant, RA

Filman, DJ

Finkel, SE

Kolter, R

Hogle, JM ^{[1
]}

机构：

[1] Harvard Univ, Sch Med, Dept Biol Chem & Mol Pharmacol, Boston, MA 02115 USA

[2] Harvard Univ, Sch Med, Dept Microbiol & Mol Genet, Boston, MA 02115 USA

[3] Harvard Univ, Comm Higher Degrees Biophys, Boston, MA 02115 USA

来源：

NATURE STRUCTURAL BIOLOGY | 1998年 / 5卷 / 04期

关键词：

D O I：

10.1038/nsb0498-294

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 Angstrom 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.

引用

收藏

页码：294 / 303

页数：10

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