View source for 7asw


==Crystal structure of chloroplastic thioredoxin z defines a novel type-specific target recognition==
<StructureSection load='7asw' size='340' side='right'caption='[[7asw]], [[Resolution|resolution]] 2.44&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7asw]] is a 1 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=7ASW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ASW 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]] 2.444&#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=7asw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7asw OCA], [https://pdbe.org/7asw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7asw RCSB], [https://www.ebi.ac.uk/pdbsum/7asw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7asw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A8J0Q8_CHLRE A8J0Q8_CHLRE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Thioredoxins (TRXs) are ubiquitous disulfide oxidoreductases structured according to a highly conserved fold. TRXs are involved in a myriad of different processes through a common chemical mechanism. Plant TRXs evolved into seven types with diverse subcellular localization and distinct protein target selectivity. Five TRX types coexist in the chloroplast, with yet scarcely described specificities. We solved the crystal structure of a chloroplastic z-type TRX, revealing a conserved TRX fold with an original electrostatic surface potential surrounding the redox site. This recognition surface is distinct from all other known TRX types from plant and non-plant sources and is exclusively conserved in plant z-type TRXs. We show that this electronegative surface endows thioredoxin z (TRXz) with a capacity to activate the photosynthetic Calvin-Benson cycle enzyme phosphoribulokinase. The distinct electronegative surface of TRXz thereby extends the repertoire of TRX-target recognitions.

Crystal structure of chloroplastic thioredoxin z defines a type-specific target recognition.,Le Moigne T, Gurrieri L, Crozet P, Marchand CH, Zaffagnini M, Sparla F, Lemaire SD, Henri J Plant J. 2021 Apr 30. doi: 10.1111/tpj.15300. PMID:33930214<ref>PMID:33930214</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7asw" style="background-color:#fffaf0;"></div>

==See Also==
*[[Thioredoxin 3D structures|Thioredoxin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Chlamydomonas reinhardtii]]
[[Category: Large Structures]]
[[Category: Crozet P]]
[[Category: Gurrieri L]]
[[Category: Henri J]]
[[Category: Le Moigne T]]
[[Category: Lemaire SD]]
[[Category: Marchand CH]]
[[Category: Sparla F]]
[[Category: Zaffagnini M]]