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==Ohr (maybe something like 'Structure')==
==Ohr ==
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
<StructureSection load='1ZB8' size='340' side='right' caption='Caption overall Ohr structure' scene=''>
This is a default text for your page '''Luis Netto/Sandbox 1'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
 
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
Ohr (Organic Hydroperoxide Resistance Protein)[[1zb8]] is a Cys based peroxidase <ref>PMID: 12540833</ref>,<ref>PMID: 12485986</ref>
 
that display higher preference for hydrogen peroxide (H2O2) than for organic hydroperoxides. Accordingly, bacteria with the gene for Ohr deleted displayed increased sensitivity for organic hydroperoxides but not for hydrogen peroxide <ref>PMID: 9573147</ref>.
 
 


== Function ==
== Function ==
Ohr is a Cys based peroxidase that means the active site Cys is very reactive towards organic hydroperoxides. This high reactivity is achieved in the active site by interactions with fully conserved Arg and Glu residues among others


== Disease ==
== Disease ==
related with relevance


== Relevance ==
== Relevance ==
Oxidants such as fatty acid hydroperoxides are signaling molecules involved in host-pathogen
interactions, and therefore, their levels are strictly controlled by peroxidases and other mechanisms
[1±4]. Ohr (Organic hydroperoxide resistance) proteins are Cys-based, dithiol-dependent
peroxidases that display unique biochemical and structural properties [5,6]. Ohr enzymes
play central roles in the bacterial response to peroxynitrite and fatty acid hydroperoxides, two
oxidants involved in host±pathogen interactions [1]. These enzymes are found in bacteria and
fungi, and they are absent in their hosts (plants and animals) [7], making them promising targets
for drug discovery. Some examples of pathogenic bacteria that express Ohr proteins are
Pseudomonas aeruginosa, Vibrio cholerae and Xyllela fastidiosa [7]. Xylella fastidiosa is a plant
pathogen with agronomic interest, causing disease in citrus, grapes and olives [8].


== Structural highlights ==
== Structural highlights ==


This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
Ohr is a homo-dimer, with a symmetrical,oval shape. The two monomers are tightly wrapped around each other in a head-to-tail orientation to generate a compact quaternary structure (Figure 1).
 
 
[[Image:Homodimer_Ohr.png|thumb|Figure1 Ohr homodimer]]
 
In Figure 1, one monomer is depicted in light blue the other in green. Reactive Cys also called peroxidatic Cys (Cp) is depicted in orange. Catalytic Arg (red) and Glu (pink) compose the catalytic triad with Cp. The catalytic Glu orientates the catalytic Arg towards Cp, increasing its nucleophilicity.
 
 
Arg19 and Glu 50 of one chain (lets say chain A) compose the  <scene name='78/785321/Catalytic_triad/1'>catalytic triad</scene> triad with Cys61 of the other chain (in this case chain  B).
 
 
The structures of Ohr in the reduced and oxidized form were also obtained. For Ohr from Xylella fastidiosa the structures of both reduced and oxidized  are available.
 
<scene name='78/785321/Oxidized_ohr/1'>Text To Be Displayed</scene>
 


</StructureSection>
== References ==
== References ==
<references/>
<references/>
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