Organic hydroperoxide resistance protein

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{{STRUCTURE_1zb8| PDB=1zb8 | SIZE=400| SCENE= |right|CAPTION=''Xylella fastidiosa'' OhrP complex with ethoxy-ethanol substrate, [[1zb8]] }}
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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'>
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'''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]].
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== Function ==
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'''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]].
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{{TOC limit|limit=2}}
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== Structural highlights ==
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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>.
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</StructureSection>
== 3D Structures of Ohr ==
== 3D Structures of Ohr ==
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
[[2pex]] – XcOhrR (mutant) reduced – ''Xanthomonas campestris''<br />
[[2pex]] – XcOhrR (mutant) reduced – ''Xanthomonas campestris''<br />
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[[3lus]] – VcOhrP + captopril – ''Vibrio cholerae''<br />
[[3lus]] – VcOhrP + captopril – ''Vibrio cholerae''<br />
[[3i07]], [[3eer]] – VcOhrP<br />
[[3i07]], [[3eer]] – VcOhrP<br />
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[[1zb8]], [[1zb9]] – OhrP – ''Xylella fastidiosa''<br />
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[[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 />
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[[1vla]] – Ohr OSMC – ''Thermotoga maritima''<br />
[[1vla]] – Ohr OSMC – ''Thermotoga maritima''<br />
[[1usp]] – OhrP – ''Deinococcus radiodurans''<br />
[[1usp]] – OhrP – ''Deinococcus radiodurans''<br />
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[[1n2f]] – OhrP – ''Pseudomonas aeruginosa''
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[[1n2f]] – OhrP – ''Pseudomonas aeruginosa''<br />
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[[4noz]] – OhrP – ''Burkholderia cenocepacia''<br />
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[[6uhw]] – OhrP – ''Burkholderia pseudomallei''<br />
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[[6d9n]] – OhrP – ''Elizabethkingia anopheles''<br />
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[[6mjn]] – OhrP – ''Legionella pneumophila''<br />
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[[6eb4]], [[6ebc]], [[6ecy]] – CvOhrP – ''Chromobacterium violaceum''<br />
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[[6ed0]] – CvOhrP (mutant)<br />
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[[6ebd]], [[6ebg]] – CvOhrP (mutant) + dihydrolipamide<br />
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Xylella fastidiosa OhrP dimer complex with PEG4000, 1zb8

Drag the structure with the mouse to rotate

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

  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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