Organic hydroperoxide resistance protein

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== Structural highlights ==
== Structural highlights ==
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OhrP is endowed by a dithiol composed of a cysteine residue and a reactive cysteine residue (cysteinesulfonic acid) able to reduce peroxide<ref>PMID:20463026</ref>.
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OhrP is endowed by a <scene name='46/461361/Cv/2'>dithiol composed of a cysteine residue and a reactive cysteine residue (cysteinesulfonic acid)</scene> able to reduce peroxide<ref>PMID:20463026</ref>.
</StructureSection>
</StructureSection>
== 3D Structures of Ohr ==
== 3D Structures of Ohr ==

Revision as of 07:19, 27 April 2017

Xylella fastidiosa OhrP dimer complex with PEG4000, 1zb8

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3D Structures of Ohr

Updated on 27-April-2017

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

  1. ↑ 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
  2. ↑ 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

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