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1ep7

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(New page: 200px<br /><applet load="1ep7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ep7, resolution 2.1&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1ep7.gif|left|200px]]<br /><applet load="1ep7" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ep7, resolution 2.1&Aring;" />
 
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'''CRYSTAL STRUCTURE OF WT THIOREDOXIN H FROM CHLAMYDOMONAS REINHARDTII'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF WT THIOREDOXIN H FROM CHLAMYDOMONAS REINHARDTII==
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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.
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<StructureSection load='1ep7' size='340' side='right'caption='[[1ep7]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ep/1ep7_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1EP7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EP7 OCA].
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*[[Thioredoxin 3D structures|Thioredoxin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=11563970 11563970]
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[[Category: Chlamydomonas reinhardtii]]
[[Category: Chlamydomonas reinhardtii]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Aubry, A.]]
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[[Category: Aubry A]]
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[[Category: Benedetti, E.]]
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[[Category: Benedetti E]]
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[[Category: Corbier, C.]]
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[[Category: Corbier C]]
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[[Category: Didierjean, C.]]
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[[Category: Didierjean C]]
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[[Category: Jacquot, J.P.]]
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[[Category: Jacquot JP]]
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[[Category: Menchise, V.]]
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[[Category: Menchise V]]
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[[Category: Saviano, M.]]
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[[Category: Saviano M]]
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[[Category: electron transport]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:11:46 2007''
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Current revision

CRYSTAL STRUCTURE OF WT THIOREDOXIN H FROM CHLAMYDOMONAS REINHARDTII

PDB ID 1ep7

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