2fe3: Difference between revisions

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[[Image:2fe3.jpg|left|200px]]<br /><applet load="2fe3" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:2fe3.jpg|left|200px]]<br /><applet load="2fe3" size="350" color="white" frame="true" align="right" spinBox="true"

caption="2fe3, resolution 1.75Å" />

'''The crystal structure of bacillus subtilis PerR-Zn reveals a novel Zn(Cys)4 Structural redox switch'''<br />

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2FE3 OCA].

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==

Line 13:

[[Category: Bacillus subtilis]]

[[Category: Single protein]]

[[Category: Traore, D.A.K.]]

[[Category: Traore, D A.K.]]

[[Category: ZN]]

[[Category: dna binding protein]]

[[Category: oxidative stress regulator]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 10:30:26 ~~2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:20:26 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2fe3.jpg|left|200px]]<br /><applet load="2fe3" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2fe3.jpg|left|200px]]<br /><applet load="2fe3" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2fe3, resolution 1.75&Aring;" />
 '''The crystal structure of bacillus subtilis PerR-Zn reveals a novel Zn(Cys)4 Structural redox switch'''<br />
 ==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.
+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==
-FE3 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FE3 OCA].
+FE3 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==
@@ Line 13: / Line 13: @@
 [[Category: Bacillus subtilis]]
 [[Category: Single protein]]
-[[Category: Traore, D.A.K.]]
+[[Category: Traore, D A.K.]]
 [[Category: ZN]]
 [[Category: dna binding protein]]
 [[Category: oxidative stress regulator]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:30:26 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:20:26 2008''