2fe3
From Proteopedia
(New page: 200px<br /><applet load="2fe3" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fe3, resolution 1.75Å" /> '''The crystal structur...) |
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| - | [[Image:2fe3.jpg|left|200px]]<br /><applet load="2fe3" size=" | + | [[Image:2fe3.jpg|left|200px]]<br /><applet load="2fe3" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2fe3, resolution 1.75Å" /> | caption="2fe3, resolution 1.75Å" /> | ||
'''The crystal structure of bacillus subtilis PerR-Zn reveals a novel Zn(Cys)4 Structural redox switch'''<br /> | '''The crystal structure of bacillus subtilis PerR-Zn reveals a novel Zn(Cys)4 Structural redox switch'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Bacteria adapt to elevated levels of Reactive Oxygen Species (ROS) by | + | Bacteria adapt to elevated levels of Reactive Oxygen Species (ROS) by increasing the expression of defence and repair proteins, which is regulated by ROS responsive transcription factors. In Bacillus subtilis the zinc protein PerR, a peroxide sensor that binds DNA in the presence of a regulatory metal Mn2+ or Fe2+, mediates the adaptive response to H2O2. This study presents the first crystal structure of apo-PerR-Zn which shows that all four cysteine residues of the protein are involved in zinc co-ordination. The Zn(Cys)4 site locks the dimerization domain and stabilizes the dimer. Sequence alignment of PerR-like proteins supports that this structural site may constitute a distinctive feature of this class of peroxide stress regulators. |
==About this Structure== | ==About this Structure== | ||
| - | 2FE3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2FE3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FE3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Traore, D | + | [[Category: Traore, D A.K.]] |
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: dna binding protein]] | [[Category: dna binding protein]] | ||
[[Category: oxidative stress regulator]] | [[Category: oxidative stress regulator]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:20:26 2008'' |
Revision as of 15:20, 21 February 2008
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The crystal structure of bacillus subtilis PerR-Zn reveals a novel Zn(Cys)4 Structural redox switch
Overview
Bacteria adapt to elevated levels of Reactive Oxygen Species (ROS) by increasing the expression of defence and repair proteins, which is regulated by ROS responsive transcription factors. In Bacillus subtilis the zinc protein PerR, a peroxide sensor that binds DNA in the presence of a regulatory metal Mn2+ or Fe2+, mediates the adaptive response to H2O2. This study presents the first crystal structure of apo-PerR-Zn which shows that all four cysteine residues of the protein are involved in zinc co-ordination. The Zn(Cys)4 site locks the dimerization domain and stabilizes the dimer. Sequence alignment of PerR-like proteins supports that this structural site may constitute a distinctive feature of this class of peroxide stress regulators.
About this Structure
2FE3 is a Single protein structure of sequence from Bacillus subtilis with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of the apo-PerR-Zn protein from Bacillus subtilis., Traore DA, El Ghazouani A, Ilango S, Dupuy J, Jacquamet L, Ferrer JL, Caux-Thang C, Duarte V, Latour JM, Mol Microbiol. 2006 Sep;61(5):1211-9. PMID:16925555
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