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[[Image:1ep7.gif|left|200px]]
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{{STRUCTURE_1ep7|  PDB=1ep7  |  SCENE=  }}
'''CRYSTAL STRUCTURE OF WT THIOREDOXIN H FROM CHLAMYDOMONAS REINHARDTII'''


==CRYSTAL STRUCTURE OF WT THIOREDOXIN H FROM CHLAMYDOMONAS REINHARDTII==
<StructureSection load='1ep7' size='340' side='right'caption='[[1ep7]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ep7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EP7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EP7 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ep7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ep7 OCA], [https://pdbe.org/1ep7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ep7 RCSB], [https://www.ebi.ac.uk/pdbsum/1ep7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ep7 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TRXH_CHLRE TRXH_CHLRE] Participates in various redox reactions through the reversible oxidation of the active center dithiol to a disulfide. The H form is known to activate a number of cytosolic enzymes.
== 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/ep/1ep7_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1ep7 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Thioredoxins are ubiquitous proteins which catalyse the reduction of disulphide bridges on target proteins. The catalytic mechanism proceeds via a mixed disulphide intermediate whose breakdown should be enhanced by the involvement of a conserved buried residue, Asp-30, as a base catalyst towards residue Cys-39. We report here the crystal structure of wild-type and D30A mutant thioredoxin h from Chlamydomonas reinhardtii, which constitutes the first crystal structure of a cytosolic thioredoxin isolated from a eukaryotic plant organism. The role of residue Asp-30 in catalysis has been revisited since the distance between the carboxylate OD1 of Asp-30 and the sulphur SG of Cys-39 is too great to support the hypothesis of direct proton transfer. A careful analysis of all available crystal structures reveals that the relative positioning of residues Asp-30 and Cys-39 as well as hydrophobic contacts in the vicinity of residue Asp-30 do not allow a conformational change sufficient to bring the two residues close enough for a direct proton transfer. This suggests that protonation/deprotonation of Cys-39 should be mediated by a water molecule. Molecular-dynamics simulations, carried out either in vacuo or in water, as well as proton-inventory experiments, support this hypothesis. The results are discussed with respect to biochemical and structural data.


==Overview==
Crystal structure of the wild-type and D30A mutant thioredoxin h of Chlamydomonas reinhardtii and implications for the catalytic mechanism.,Menchise V, Corbier C, Didierjean C, Saviano M, Benedetti E, Jacquot JP, Aubry A Biochem J. 2001 Oct 1;359(Pt 1):65-75. PMID:11563970<ref>PMID:11563970</ref>
Thioredoxins are ubiquitous proteins which catalyse the reduction of disulphide bridges on target proteins. The catalytic mechanism proceeds via a mixed disulphide intermediate whose breakdown should be enhanced by the involvement of a conserved buried residue, Asp-30, as a base catalyst towards residue Cys-39. We report here the crystal structure of wild-type and D30A mutant thioredoxin h from Chlamydomonas reinhardtii, which constitutes the first crystal structure of a cytosolic thioredoxin isolated from a eukaryotic plant organism. The role of residue Asp-30 in catalysis has been revisited since the distance between the carboxylate OD1 of Asp-30 and the sulphur SG of Cys-39 is too great to support the hypothesis of direct proton transfer. A careful analysis of all available crystal structures reveals that the relative positioning of residues Asp-30 and Cys-39 as well as hydrophobic contacts in the vicinity of residue Asp-30 do not allow a conformational change sufficient to bring the two residues close enough for a direct proton transfer. This suggests that protonation/deprotonation of Cys-39 should be mediated by a water molecule. Molecular-dynamics simulations, carried out either in vacuo or in water, as well as proton-inventory experiments, support this hypothesis. The results are discussed with respect to biochemical and structural data.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1EP7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EP7 OCA].
</div>
<div class="pdbe-citations 1ep7" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Crystal structure of the wild-type and D30A mutant thioredoxin h of Chlamydomonas reinhardtii and implications for the catalytic mechanism., Menchise V, Corbier C, Didierjean C, Saviano M, Benedetti E, Jacquot JP, Aubry A, Biochem J. 2001 Oct 1;359(Pt 1):65-75. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11563970 11563970]
*[[Thioredoxin 3D structures|Thioredoxin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Chlamydomonas reinhardtii]]
[[Category: Chlamydomonas reinhardtii]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Aubry, A.]]
[[Category: Aubry A]]
[[Category: Benedetti, E.]]
[[Category: Benedetti E]]
[[Category: Corbier, C.]]
[[Category: Corbier C]]
[[Category: Didierjean, C.]]
[[Category: Didierjean C]]
[[Category: Jacquot, J P.]]
[[Category: Jacquot JP]]
[[Category: Menchise, V.]]
[[Category: Menchise V]]
[[Category: Saviano, M.]]
[[Category: Saviano M]]
[[Category: Electron transport]]
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Retrieved from "https://proteopedia.org/1ep7"