1dps: Difference between revisions

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




==Overview==
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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.
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{{ABSTRACT_PUBMED_9546221}}


==About this Structure==
==About this Structure==
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[[Category: Oxidative damage]]
[[Category: Oxidative damage]]
[[Category: Stationary phase]]
[[Category: Stationary phase]]
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Revision as of 23:26, 30 June 2008

File:1dps.png

Template:STRUCTURE 1dps

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

Template:ABSTRACT PUBMED 9546221

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

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