Organic hydroperoxide resistance protein
From Proteopedia
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| - | + | <StructureSection load='' size='350' side='right' scene='46/461361/Cv/1' caption='Xylella fastidiosa OhrP dimer complex with PEG4000, [[1zb8]]' pspeed='8'> | |
| - | '''Organic hydroperoxide resistance protein''' (OhrP) is a peroxidase involved in bacterial stress induced by organic hydroperoxides. OhrP requires dithiols for its activity. | + | == Function == |
| - | + | '''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]]. | |
| - | + | ||
| + | == Structural highlights == | ||
| + | OhrP is endowed by a <scene name='46/461361/Cv/3'>dithiol composed of a cysteine residue and a reactive cysteine residue (cysteinesulfonic acid)</scene> able to reduce peroxide<ref>PMID:20463026</ref>. | ||
| + | </StructureSection> | ||
== 3D Structures of Ohr == | == 3D Structures of Ohr == | ||
| - | [[2pex]] – XcOhrR (mutant) reduced – Xanthomonas campestris<br /> | + | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} |
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| + | [[2pex]] – XcOhrR (mutant) reduced – ''Xanthomonas campestris''<br /> | ||
[[2pfb]] - XcOhrR (mutant) oxidized<br /> | [[2pfb]] - XcOhrR (mutant) oxidized<br /> | ||
| - | [[3lus]] – VcOhrP + captopril – Vibrio cholerae<br /> | + | [[3lus]] – VcOhrP + captopril – ''Vibrio cholerae''<br /> |
[[3i07]], [[3eer]] – VcOhrP<br /> | [[3i07]], [[3eer]] – VcOhrP<br /> | ||
| - | [[1zb8]], [[1zb9]] – OhrP – Xylella fastidiosa<br /> | + | [[1zb8]], [[1zb9]], [[4xx2]] – OhrP – ''Xylella fastidiosa''<br /> |
| - | [[2bjo]] – BsOhrB – Bacillus subtilis<br /> | + | [[2bjo]] – BsOhrB – ''Bacillus subtilis''<br /> |
[[1z91]] – BsOhrRC15S (mutant) reduced<br /> | [[1z91]] – BsOhrRC15S (mutant) reduced<br /> | ||
[[1z9c]] – BsOhrA + DNA<br /> | [[1z9c]] – BsOhrA + DNA<br /> | ||
| - | [[1vla]] – Ohr OSMC – Thermotoga maritima<br /> | + | [[1vla]] – Ohr OSMC – ''Thermotoga maritima''<br /> |
| - | [[1usp]] – OhrP – Deinococcus radiodurans<br /> | + | [[1usp]] – OhrP – ''Deinococcus radiodurans''<br /> |
| - | [[1n2f]] – OhrP – Pseudomonas aeruginosa | + | [[1n2f]] – OhrP – ''Pseudomonas aeruginosa''<br /> |
| + | [[4noz]] – OhrP – ''Burkholderia cenocepacia''<br /> | ||
| + | [[6uhw]] – OhrP – ''Burkholderia pseudomallei''<br /> | ||
| + | [[6d9n]] – OhrP – ''Elizabethkingia anopheles''<br /> | ||
| + | [[6mjn]] – OhrP – ''Legionella pneumophila''<br /> | ||
| + | [[6eb4]], [[6ebc]], [[6ecy]] – CvOhrP – ''Chromobacterium violaceum''<br /> | ||
| + | [[6ed0]] – CvOhrP (mutant)<br /> | ||
| + | [[6ebd]], [[6ebg]] – CvOhrP (mutant) + dihydrolipamide<br /> | ||
| + | == References == | ||
| + | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Current revision
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3D Structures of Ohr
Updated on 16-September-2020
2pex – XcOhrR (mutant) reduced – Xanthomonas campestris
2pfb - XcOhrR (mutant) oxidized
3lus – VcOhrP + captopril – Vibrio cholerae
3i07, 3eer – VcOhrP
1zb8, 1zb9, 4xx2 – 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
6uhw – OhrP – Burkholderia pseudomallei
6d9n – OhrP – Elizabethkingia anopheles
6mjn – OhrP – Legionella pneumophila
6eb4, 6ebc, 6ecy – CvOhrP – Chromobacterium violaceum
6ed0 – CvOhrP (mutant)
6ebd, 6ebg – CvOhrP (mutant) + dihydrolipamide
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
- ↑ 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
