1umn

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[[Image:1umn.jpg|left|200px]]<br /><applet load="1umn" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1umn.jpg|left|200px]]
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caption="1umn, resolution 1.95&Aring;" />
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'''CRYSTAL STRUCTURE OF DPS-LIKE PEROXIDE RESISTANCE PROTEIN (DPR) FROM STREPTOCOCCUS SUIS'''<br />
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{{Structure
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|PDB= 1umn |SIZE=350|CAPTION= <scene name='initialview01'>1umn</scene>, resolution 1.95&Aring;
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|SITE= <scene name='pdbsite=C01:Ca+Binding+Site+For+Chain+K'>C01</scene>
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID'>EPE</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF DPS-LIKE PEROXIDE RESISTANCE PROTEIN (DPR) FROM STREPTOCOCCUS SUIS'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1UMN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_suis Streptococcus suis] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=EPE:'>EPE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=C01:Ca+Binding+Site+For+Chain+K'>C01</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UMN OCA].
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1UMN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_suis Streptococcus suis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UMN OCA].
==Reference==
==Reference==
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Crystal structure of Streptococcus suis Dps-like peroxide resistance protein Dpr: implications for iron incorporation., Kauko A, Haataja S, Pulliainen AT, Finne J, Papageorgiou AC, J Mol Biol. 2004 Apr 30;338(3):547-58. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15081812 15081812]
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Crystal structure of Streptococcus suis Dps-like peroxide resistance protein Dpr: implications for iron incorporation., Kauko A, Haataja S, Pulliainen AT, Finne J, Papageorgiou AC, J Mol Biol. 2004 Apr 30;338(3):547-58. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15081812 15081812]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Streptococcus suis]]
[[Category: Streptococcus suis]]
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[[Category: peroxide resistance]]
[[Category: peroxide resistance]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:26:10 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:34:01 2008''

Revision as of 12:34, 20 March 2008

Image:1umn.jpg


PDB ID 1umn

Drag the structure with the mouse to rotate
, resolution 1.95Å
Sites:
Ligands: , and
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF DPS-LIKE PEROXIDE RESISTANCE PROTEIN (DPR) FROM STREPTOCOCCUS SUIS


Overview

The Dps-like peroxide resistance protein (Dpr) is an aerotolerance and hydrogen peroxide resistance agent found in the meningitis-associated pathogen Streptococcus suis. Dpr is believed to act by binding free intracellular iron to prevent Fenton chemistry-catalysed formation of toxic hydroxyl radicals. The crystal structure of Dpr has been determined to 1.95 A resolution. The final model has an Rcyst value of 18.5% (Rfree = 22.4%) and consists of 12 identical monomers (each of them comprising a four alpha-helix bundle) that form a hollow sphere obeying 23 symmetry. Structural features show that Dpr belongs to the Dps family of bacterial proteins. Twelve putative ferroxidase centers, each formed at the interface of neighboring monomer pairs, were identified in the Dpr structure with structural similarities to those found in other Dps family members. Dpr was crystallized in the absence of iron, hence no bound iron was found in the structure in contrast to other Dps family members. A novel metal-binding site approximately 6A from the ferroxidase centre was identified and assigned to a bound calcium ion. Two residues from the ferroxidase centre (Asp63 and Asp74) were found to be involved in calcium binding. Structural comparison with other family members revealed that Asp63 and Asp74 adopt different conformation in the Dpr structure. The structure of Dpr presented here shows potential local conformational changes that may occur during iron incorporation. A role for the metal-binding site in iron uptake is proposed.

About this Structure

1UMN is a Single protein structure of sequence from Streptococcus suis. Full crystallographic information is available from OCA.

Reference

Crystal structure of Streptococcus suis Dps-like peroxide resistance protein Dpr: implications for iron incorporation., Kauko A, Haataja S, Pulliainen AT, Finne J, Papageorgiou AC, J Mol Biol. 2004 Apr 30;338(3):547-58. PMID:15081812

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