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Ohr

spinqualitylabelsall models Caption overall Ohr structure Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Ohr (Organic Hydroperoxide Resistance Protein)1zb8 is a Cys based peroxidase , 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 . 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') Anything in this section will appear adjacent to the 3D structure and will be scrollable.

It is involved in the response of

Disease

related with 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

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.

Figure1 Ohr homodimer

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

Arg19 and Glu 50 of one chain (lets say chain A) compose the catalytic triad triad with Cys61 of the other chain (in this case chain B).

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Luis Netto