5nym

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:27, 1 May 2024) (edit) (undo)
 
(2 intermediate revisions not shown.)
Line 1: Line 1:
==Crystal structure of the atypical poplar thioredoxin-like2.1 in reduced state==
==Crystal structure of the atypical poplar thioredoxin-like2.1 in reduced state==
-
<StructureSection load='5nym' size='340' side='right' caption='[[5nym]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
+
<StructureSection load='5nym' size='340' side='right'caption='[[5nym]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5nym]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Hybrid_aspen Hybrid aspen]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NYM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NYM FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5nym]] 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=5NYM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NYM 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=SO4:SULFATE+ION'>SO4</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5nyk|5nyk]], [[5nyl|5nyl]], [[5nyn|5nyn]], [[5nyo|5nyo]]</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=SO4:SULFATE+ION'>SO4</scene></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=5nym FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nym OCA], [http://pdbe.org/5nym PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nym RCSB], [http://www.ebi.ac.uk/pdbsum/5nym PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nym ProSAT]</span></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=5nym FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nym OCA], [https://pdbe.org/5nym PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nym RCSB], [https://www.ebi.ac.uk/pdbsum/5nym PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nym ProSAT]</span></td></tr>
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/I0BZV0_POPPZ I0BZV0_POPPZ]
-
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 5nym" style="background-color:#fffaf0;"></div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Hybrid aspen]]
+
[[Category: Large Structures]]
-
[[Category: Chibani, K]]
+
[[Category: Populus tremula x Populus tremuloides]]
-
[[Category: Haouz, A]]
+
[[Category: Chibani K]]
-
[[Category: Rouhier, N]]
+
[[Category: Haouz A]]
-
[[Category: Saul, F A]]
+
[[Category: Rouhier N]]
-
[[Category: Atypical thioredoxin]]
+
[[Category: Saul FA]]
-
[[Category: Disulfide exchange]]
+
-
[[Category: Oxidoreductase]]
+

Current revision

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

PDB ID 5nym

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools