1dps

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(New page: 200px<br /><applet load="1dps" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dps, resolution 1.60&Aring;" /> '''THE CRYSTAL STRUCTUR...)
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[[Image:1dps.jpg|left|200px]]<br /><applet load="1dps" size="350" color="white" frame="true" align="right" spinBox="true"
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caption="1dps, resolution 1.60&Aring;" />
'''THE CRYSTAL STRUCTURE OF DPS, A FERRITIN HOMOLOG THAT BINDS AND PROTECTS DNA'''<br />
'''THE CRYSTAL STRUCTURE OF DPS, A FERRITIN HOMOLOG THAT BINDS AND PROTECTS DNA'''<br />
==Overview==
==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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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 Structure==
==About this Structure==
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1DPS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with NA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DPS OCA].
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1DPS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=NA:'>NA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DPS OCA].
==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Filman, D.J.]]
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[[Category: Filman, D J.]]
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[[Category: Finkel, S.E.]]
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[[Category: Finkel, S E.]]
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[[Category: Grant, R.A.]]
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[[Category: Grant, R A.]]
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[[Category: Hogle, J.M.]]
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[[Category: Hogle, J M.]]
[[Category: Kolter, R.]]
[[Category: Kolter, R.]]
[[Category: NA]]
[[Category: NA]]
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[[Category: stationary phase]]
[[Category: stationary phase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:28:53 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:19:10 2008''

Revision as of 10:19, 21 February 2008


1dps, resolution 1.60Å

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

Overview

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 Structure

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

Reference

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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