4aec

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[[Image:4aec.png|left|200px]]
 
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==Crystal Structure of the Arabidopsis thaliana O-Acetyl-Serine-(Thiol)- Lyase C==
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The line below this paragraph, containing "STRUCTURE_4aec", creates the "Structure Box" on the page.
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<StructureSection load='4aec' size='340' side='right' caption='[[4aec]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[4aec]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AEC FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cysteine_synthase Cysteine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.47 2.5.1.47] </span></td></tr>
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{{STRUCTURE_4aec| PDB=4aec | SCENE= }}
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<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=4aec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aec OCA], [http://pdbe.org/4aec PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4aec RCSB], [http://www.ebi.ac.uk/pdbsum/4aec PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4aec ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===Crystal Structure of the Arabidopsis thaliana O-Acetyl-Serine-(Thiol)- Lyase C===
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The line below this paragraph, {{ABSTRACT_PUBMED_22325778}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 4aec" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 22325778 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_22325778}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Arath]]
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[[4aec]] is a 2 chain structure with sequence from [http://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].
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==Reference==
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<ref group="xtra">PMID:022325778</ref><references group="xtra"/>
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[[Category: Arabidopsis thaliana]]
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[[Category: Cysteine synthase]]
[[Category: Cysteine synthase]]
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[[Category: Feldman-Salit, A.]]
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[[Category: Feldman-Salit, A]]
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[[Category: Hell, R.]]
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[[Category: Hell, R]]
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[[Category: Hothorn, M.]]
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[[Category: Hothorn, M]]
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[[Category: Lenherr, E D.]]
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[[Category: Lenherr, E D]]
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[[Category: Scheffzek, K.]]
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[[Category: Scheffzek, K]]
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[[Category: Throm, C.]]
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[[Category: Throm, C]]
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[[Category: Wade, R C.]]
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[[Category: Wade, R C]]
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[[Category: Wirtz, M.]]
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[[Category: Wirtz, M]]
[[Category: Assimilatory sulfate reduction]]
[[Category: Assimilatory sulfate reduction]]
[[Category: Cysteine synthesis]]
[[Category: Cysteine synthesis]]

Revision as of 10:06, 4 August 2016

Crystal Structure of the Arabidopsis thaliana O-Acetyl-Serine-(Thiol)- Lyase C

4aec, resolution 2.40Å

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