View source for 5nyk


==Crystal structure of the atypical poplar thioredoxin-like2.1 in oxidized state==
<StructureSection load='5nyk' size='340' side='right'caption='[[5nyk]], [[Resolution|resolution]] 1.05&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5nyk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Populus_tremula_x_Populus_tremuloides Populus tremula x Populus tremuloides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NYK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NYK 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]] 1.05&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=5nyk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nyk OCA], [https://pdbe.org/5nyk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nyk RCSB], [https://www.ebi.ac.uk/pdbsum/5nyk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nyk ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/I0BZV0_POPPZ I0BZV0_POPPZ] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Plastidial thioredoxin (TRX)-like2.1 proteins are atypical thioredoxins possessing a WCRKC active site signature and using glutathione for recycling. To obtain structural information supporting the peculiar catalytic mechanisms and target proteins of these TRXs, we solved the crystal structures of poplar TRX-like2.1 in oxidized and reduced states and of mutated variants. These structures share similar folding with TRXs exhibiting the canonical WCGPC signature. Moreover, the overall conformation is not altered by reduction of the catalytic disulfide bond or in a C45S/C67S variant that formed a disulfide-bridged dimer possibly mimicking reaction intermediates with target proteins. Modelling of the interaction of TRX-like2.1 with both NADPH- and ferredoxin-thioredoxin reductases indicates that the presence of Arg43 and Lys44 residues likely precludes reduction by the plastidial ferredoxin-thioredoxin reductase. This article is protected by copyright. All rights reserved.

Structural snapshots along the reaction mechanism of the atypical poplar thioredoxin-like2.1.,Chibani K, Saul F, Didierjean C, Rouhier N, Haouz A FEBS Lett. 2018 Feb 17. doi: 10.1002/1873-3468.13009. PMID:29453875<ref>PMID:29453875</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5nyk" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Populus tremula x Populus tremuloides]]
[[Category: Chibani K]]
[[Category: Haouz A]]
[[Category: Rouhier N]]
[[Category: Saul FA]]