Organic hydroperoxide resistance protein
From Proteopedia
(Difference between revisions)
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{{STRUCTURE_1zb8| PDB=1zb8 | SIZE=350| SCENE= |right|CAPTION=''Xylella fastidiosa'' OhrP dimer complex with ethoxy-ethanol substrate, [[1zb8]] }} | {{STRUCTURE_1zb8| PDB=1zb8 | SIZE=350| SCENE= |right|CAPTION=''Xylella fastidiosa'' OhrP dimer complex with ethoxy-ethanol substrate, [[1zb8]] }} | ||
- | '''Organic hydroperoxide resistance protein''' (OhrP) is a peroxidase involved in bacterial stress induced by organic hydroperoxides. OhrP requires dithiols for its activity. For ''Xanthomonas campestris'' OhrR see [[OhrR]]. | + | '''Organic hydroperoxide resistance protein''' (OhrP) is a peroxidase involved in bacterial stress induced by organic hydroperoxides. OhrP requires dithiols for its activity<ref>PMID:20463026</ref>. For ''Xanthomonas campestris'' OhrR see [[OhrR]]. |
== 3D Structures of Ohr == | == 3D Structures of Ohr == | ||
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[[4noz]] – OhrP – ''Burkholderia cenocepacia''<br /> | [[4noz]] – OhrP – ''Burkholderia cenocepacia''<br /> | ||
+ | == References == | ||
+ | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] |
Revision as of 08:51, 9 June 2016
Organic hydroperoxide resistance protein (OhrP) is a peroxidase involved in bacterial stress induced by organic hydroperoxides. OhrP requires dithiols for its activity[1]. For Xanthomonas campestris OhrR see OhrR.
3D Structures of Ohr
Updated on 09-June-2016
2pex – XcOhrR (mutant) reduced – Xanthomonas campestris
2pfb - XcOhrR (mutant) oxidized
3lus – VcOhrP + captopril – Vibrio cholerae
3i07, 3eer – VcOhrP
1zb8, 1zb9 – OhrP – Xylella fastidiosa
2bjo – BsOhrB – Bacillus subtilis
1z91 – BsOhrRC15S (mutant) reduced
1z9c – BsOhrA + DNA
1vla – Ohr OSMC – Thermotoga maritima
1usp – OhrP – Deinococcus radiodurans
1n2f – OhrP – Pseudomonas aeruginosa
4noz – OhrP – Burkholderia cenocepacia
References
- ↑ Cussiol JR, Alegria TG, Szweda LI, Netto LE. Ohr (organic hydroperoxide resistance protein) possesses a previously undescribed activity, lipoyl-dependent peroxidase. J Biol Chem. 2010 Jul 16;285(29):21943-50. doi: 10.1074/jbc.M110.117283. Epub, 2010 May 12. PMID:20463026 doi:http://dx.doi.org/10.1074/jbc.M110.117283