User:Luis Netto/Sandbox 1: Difference between revisions

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Ohr (Organic Hydroperoxide Resistance Protein)[[1zb8]] is a Cys based peroxidase <ref>PMID: 12540833</ref>,<ref>PMID: 12485986</ref>
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 than for organic hydroperoxides.  
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.
 
 
 
 
 
 
 
 
Ohr is a tight homo-dimer a  [[Image:Ohr_black_white.png | thumb]]
 


It is involved in the response of


Ohr is a dimer glu arg in the active site [[Image:Ohr_black_white.png | thumb]]
glu arg in the active site




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== 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==Your Heading Here (maybe something like 'Structure')==
<StructureSection load='1ZB8' size='350' side='right' caption='Escherichia coli reca protein-bound DNA (PDB entry [[3rec]])' scene=''>
Anything in this section will appear adjacent to the 3D structure and will be scrollable.
</StructureSection>
It is involved in the response of


== Disease ==
== Disease ==

Revision as of 00:12, 30 May 2018

OhrOhr


Ohr (Organic Hydroperoxide Resistance Protein)1zb8 is a Cys based peroxidase [1],[2]

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.





Ohr is a tight homo-dimer a


glu arg in the active site



This is a default text for your page Luis Netto/Sandbox 1. Click above on edit this page to modify. Be careful with the < and > signs.

You may include any references to papers as in: the use of JSmol in Proteopedia [3] or to the article describing Jmol [4] to the rescue.

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==Your Heading Here (maybe something like 'Structure')==

<StructureSection load='1ZB8' size='350' side='right' caption='Escherichia coli reca protein-bound DNA (PDB entry 3rec)' scene=>

Anything in this section will appear adjacent to the 3D structure and will be scrollable.


Caption for this structure

Drag the structure with the mouse to rotate


It is involved in the response of

DiseaseDisease

RelevanceRelevance

Structural highlightsStructural highlights

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>

ReferencesReferences

  1. Cussiol JR, Alves SV, de Oliveira MA, Netto LE. Organic hydroperoxide resistance gene encodes a thiol-dependent peroxidase. J Biol Chem. 2003 Mar 28;278(13):11570-8. doi: 10.1074/jbc.M300252200. Epub 2003 , Jan 22. PMID:12540833 doi:http://dx.doi.org/10.1074/jbc.M300252200
  2. Lesniak J, Barton WA, Nikolov DB. Structural and functional characterization of the Pseudomonas hydroperoxide resistance protein Ohr. EMBO J. 2002 Dec 16;21(24):6649-59. PMID:12485986
  3. Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  4. Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644