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[[Image:1tp9.gif|left|200px]]


{{Structure
==PRX D (type II) from Populus tremula==
|PDB= 1tp9 |SIZE=350|CAPTION= <scene name='initialview01'>1tp9</scene>, resolution 1.62&Aring;
<StructureSection load='1tp9' size='340' side='right'caption='[[1tp9]], [[Resolution|resolution]] 1.62&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
<table><tr><td colspan='2'>[[1tp9]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Populus_trichocarpa Populus trichocarpa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TP9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TP9 FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.62&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tp9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tp9 OCA], [https://pdbe.org/1tp9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tp9 RCSB], [https://www.ebi.ac.uk/pdbsum/1tp9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tp9 ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tp9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tp9 OCA], [http://www.ebi.ac.uk/pdbsum/1tp9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tp9 RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/PRX2_POPTR PRX2_POPTR] Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. Plays a role in cell protection against oxidative stress by detoxifying peroxides.<ref>PMID:15032877</ref> <ref>PMID:18230180</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tp/1tp9_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1tp9 ConSurf].
<div style="clear:both"></div>


'''PRX D (type II) from Populus tremula'''
==See Also==
 
*[[Peroxiredoxin 3D structures|Peroxiredoxin 3D structures]]
 
== References ==
==Overview==
<references/>
Peroxiredoxins (Prxs) constitute a family of thiol peroxidases that reduce hydrogen peroxide, peroxinitrite, and hydroperoxides using a strictly conserved cysteine. Very abundant in all organisms, Prxs are produced as diverse isoforms characterized by different catalytic mechanisms and various thiol-containing reducing agents. The oligomeric state of Prxs and the link with their functionality is a subject of intensive research. We present here a combined X-ray and nuclear magnetic resonance (NMR) study of a plant Prx that belongs to the D-Prx (type II) subfamily. The Populus trichocarpa Prx is the first Prx shown to be regenerated in vitro by both the glutaredoxin and thioredoxin systems. The crystal structure and solution NMR provide evidence that the reduced protein is a specific noncovalent homodimer both in the crystal and in solution. The dimer interface is roughly perpendicular to the plane of the central beta sheet and differs from the interface of A- and B-Prx dimers, where proteins associate in the plane parallel to the beta sheet. The homodimer interface involves residues strongly conserved in the D (type II) Prxs, suggesting that all Prxs of this family can homodimerize. The study provides a new insight into the Prx oligomerism and the basis for protein-protein and enzyme-substrate interaction studies by NMR.
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1TP9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Populus_trichocarpa Populus trichocarpa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TP9 OCA].
 
==Reference==
Crystal structure and solution NMR dynamics of a D (type II) peroxiredoxin glutaredoxin and thioredoxin dependent: a new insight into the peroxiredoxin oligomerism., Echalier A, Trivelli X, Corbier C, Rouhier N, Walker O, Tsan P, Jacquot JP, Aubry A, Krimm I, Lancelin JM, Biochemistry. 2005 Feb 15;44(6):1755-67. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15697201 15697201]
[[Category: Populus trichocarpa]]
[[Category: Populus trichocarpa]]
[[Category: Single protein]]
[[Category: Corbier C]]
[[Category: Corbier, C.]]
[[Category: Echalier A]]
[[Category: Echalier, A.]]
[[Category: Jacquot JP]]
[[Category: Jacquot, J P.]]
[[Category: Krimm I]]
[[Category: Krimm, I.]]
[[Category: Lancelin JM]]
[[Category: Lancelin, J M.]]
[[Category: Rouhier N]]
[[Category: Rouhier, N.]]
[[Category: Trivelli X]]
[[Category: Trivelli, X.]]
[[Category: Tsan P]]
[[Category: Tsan, P.]]
[[Category: Walker O]]
[[Category: Walker, O.]]
[[Category: oligomer]]
[[Category: peroxiredoxin]]
[[Category: thioredoxin fold]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:59:13 2008''

Latest revision as of 16:30, 13 March 2024

PRX D (type II) from Populus tremulaPRX D (type II) from Populus tremula

Structural highlights

1tp9 is a 4 chain structure with sequence from Populus trichocarpa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.62Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PRX2_POPTR Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. Plays a role in cell protection against oxidative stress by detoxifying peroxides.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Rouhier N, Gelhaye E, Corbier C, Jacquot JP. Active site mutagenesis and phospholipid hydroperoxide reductase activity of poplar type II peroxiredoxin. Physiol Plant. 2004 Jan;120(1):57-62. PMID:15032877 doi:10.1111/j.0031-9317.2004.0203.x
  2. ↑ Ralph SG, Chun HJ, Cooper D, Kirkpatrick R, Kolosova N, Gunter L, Tuskan GA, Douglas CJ, Holt RA, Jones SJ, Marra MA, Bohlmann J. Analysis of 4,664 high-quality sequence-finished poplar full-length cDNA clones and their utility for the discovery of genes responding to insect feeding. BMC Genomics. 2008 Jan 29;9:57. PMID:18230180 doi:10.1186/1471-2164-9-57

1tp9, resolution 1.62Å

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