9ufc: Difference between revisions

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'''Unreleased structure'''


The entry 9ufc is ON HOLD
==Structural of a glutamate cysteine ligase StGSH1 in Solanum tuberosum==
<StructureSection load='9ufc' size='340' side='right'caption='[[9ufc]], [[Resolution|resolution]] 2.53&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9ufc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Solanum_tuberosum Solanum tuberosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9UFC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9UFC 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]] 2.53&#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=9ufc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9ufc OCA], [https://pdbe.org/9ufc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9ufc RCSB], [https://www.ebi.ac.uk/pdbsum/9ufc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9ufc ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Glutathione (GSH) plays a crucial role in plant metabolism and stress response. The rate-limiting step in the biosynthesis of GSH is catalyzed by glutamate cysteine ligase (GCL) the activity of which is tightly regulated. The regulation of plant GCLs is poorly understood. The crystal structure of substrate-bound GCL from Brassica juncea at 2.1-A resolution reveals a plant-unique regulatory mechanism based on two intramolecular redox-sensitive disulfide bonds. Reduction of one disulfide bond allows a beta-hairpin motif to shield the active site of B. juncea GCL, thereby preventing the access of substrates. Reduction of the second disulfide bond reversibly controls dimer to monomer transition of B. juncea GCL that is associated with a significant inactivation of the enzyme. These regulatory events provide a molecular link between high GSH levels in the plant cell and associated down-regulation of its biosynthesis. Furthermore, known mutations in the Arabidopsis GCL gene affect residues in the close proximity of the active site and thus explain the decreased GSH levels in mutant plants. In particular, the mutation in rax1-1 plants causes impaired binding of cysteine.


Authors: Zhao, H.B., Fan, S.L.
Structural basis for the redox control of plant glutamate cysteine ligase.,Hothorn M, Wachter A, Gromes R, Stuwe T, Rausch T, Scheffzek K J Biol Chem. 2006 Sep 15;281(37):27557-65. Epub 2006 Jun 9. PMID:16766527<ref>PMID:16766527</ref>


Description: Structural of a glutamate cysteine ligase StGSH1 in Solanum tuberosum
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Zhao, H.B]]
<div class="pdbe-citations 9ufc" style="background-color:#fffaf0;"></div>
[[Category: Fan, S.L]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Solanum tuberosum]]
[[Category: Fan SL]]
[[Category: Zhao HB]]

Latest revision as of 09:31, 15 April 2026

Structural of a glutamate cysteine ligase StGSH1 in Solanum tuberosum

9ufc, resolution 2.53Å

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