5nyk

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "5nyk" [edit=sysop:move=sysop])
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 5nyk is ON HOLD
+
==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. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NYK FirstGlance]. <br>
 +
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5nyl|5nyl]], [[5nym|5nym]], [[5nyn|5nyn]], [[5nyo|5nyo]]</td></tr>
 +
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5nyk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nyk OCA], [http://pdbe.org/5nyk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nyk RCSB], [http://www.ebi.ac.uk/pdbsum/5nyk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nyk ProSAT]</span></td></tr>
 +
</table>
 +
<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.
-
Authors: Chibani, K., Saul, F.A., Haouz, A., Rouhier, N.
+
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>
-
Description: Crystal structure of the atypical poplar thioredoxin-like2.1 in oxidized state
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
[[Category: Unreleased Structures]]
+
</div>
 +
<div class="pdbe-citations 5nyk" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
[[Category: Chibani, K]]
[[Category: Chibani, K]]
-
[[Category: Rouhier, N]]
 
-
[[Category: Saul, F.A]]
 
[[Category: Haouz, A]]
[[Category: Haouz, A]]
 +
[[Category: Rouhier, N]]
 +
[[Category: Saul, F A]]
 +
[[Category: Atypical thioredoxin]]
 +
[[Category: Disulfide exchange]]
 +
[[Category: Oxidoreductase]]

Revision as of 06:18, 28 February 2018

Crystal structure of the atypical poplar thioredoxin-like2.1 in oxidized state

5nyk, resolution 1.05Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools