1umn
From Proteopedia
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| - | [[Image:1umn. | + | [[Image:1umn.jpg|left|200px]]<br /><applet load="1umn" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1umn" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1umn, resolution 1.95Å" /> | caption="1umn, resolution 1.95Å" /> | ||
'''CRYSTAL STRUCTURE OF DPS-LIKE PEROXIDE RESISTANCE PROTEIN (DPR) FROM STREPTOCOCCUS SUIS'''<br /> | '''CRYSTAL STRUCTURE OF DPS-LIKE PEROXIDE RESISTANCE PROTEIN (DPR) FROM STREPTOCOCCUS SUIS'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 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 CA, CL and EPE as [http://en.wikipedia.org/wiki/ligands ligands]. | + | 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 CA, CL and EPE 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UMN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: peroxide resistance]] | [[Category: peroxide resistance]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:03:27 2007'' |
Revision as of 15:53, 18 December 2007
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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 with CA, CL and EPE as ligands. Known structural/functional Site: . 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
Page seeded by OCA on Tue Dec 18 18:03:27 2007
Categories: Single protein | Streptococcus suis | Finne, J. | Haataja, S. | Kauko, A. | Papageorgiou, A.C. | Pulliainen, A. | CA | CL | EPE | Dps-family | Ferritin-like | Ferroxidase | Iron-binding | Peroxide resistance
