4aec: Difference between revisions
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New page: '''Unreleased structure''' The entry 4aec is ON HOLD Authors: Feldman-Salit, A., Wirtz, M., Lenherr, E.D., Throm, C., Hothorn, M., Scheffzek, K., Hell, R., Wade, R.C. Description: Crys... |
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The | ==Crystal Structure of the Arabidopsis thaliana O-Acetyl-Serine-(Thiol)- Lyase C== | ||
<StructureSection load='4aec' size='340' side='right'caption='[[4aec]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4aec]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AEC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AEC 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]] 2.4Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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=4aec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aec OCA], [https://pdbe.org/4aec PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4aec RCSB], [https://www.ebi.ac.uk/pdbsum/4aec PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4aec ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CYSKM_ARATH CYSKM_ARATH] Acts as a cysteine synthase. Plays a role in the sulfide detoxification in mitochondria.<ref>PMID:18024555</ref> <ref>PMID:18223034</ref> <ref>PMID:22511607</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Plants and bacteria assimilate sulfur into cysteine. Cysteine biosynthesis involves a bienzyme complex, the cysteine synthase complex (CSC), which consists of serine-acetyl-transferase (SAT) and O-acetyl-serine-(thiol)-lyase (OAS-TL) enzymes. The activity of OAS-TL is reduced by formation of the CSC. Although this reduction is an inherent part of the self-regulation cycle of cysteine biosynthesis, there has until now been no explanation as to how OAS-TL loses activity in plants. Complexation of SAT and OAS-TL involves binding of the C-terminal tail of SAT in one of the active sites of the homodimeric OAS-TL. We here explore the flexibility of the unoccupied active site in Arabidopsis thaliana cytosolic and mitochondrial OAS-TLs. Our results reveal two gates in the OAS-TL active site that define its accessibility. The observed dynamics of the gates show allosteric closure of the unoccupied active site of OAS-TL in the CSC, which can hinder substrate binding, abolishing its turnover to cysteine. | |||
Allosterically Gated Enzyme Dynamics in the Cysteine Synthase Complex Regulate Cysteine Biosynthesis in Arabidopsis thaliana.,Feldman-Salit A, Wirtz M, Lenherr ED, Throm C, Hothorn M, Scheffzek K, Hell R, Wade RC Structure. 2012 Feb 8;20(2):292-302. PMID:22325778<ref>PMID:22325778</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4aec" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Arabidopsis thaliana]] | |||
[[Category: Large Structures]] | |||
[[Category: Feldman-Salit A]] | |||
[[Category: Hell R]] | |||
[[Category: Hothorn M]] | |||
[[Category: Lenherr ED]] | |||
[[Category: Scheffzek K]] | |||
[[Category: Throm C]] | |||
[[Category: Wade RC]] | |||
[[Category: Wirtz M]] | |||
Latest revision as of 11:25, 20 December 2023
Crystal Structure of the Arabidopsis thaliana O-Acetyl-Serine-(Thiol)- Lyase C
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