This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


4aec

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (11:25, 20 December 2023) (edit) (undo)
 
(4 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:4aec.png|left|200px]]
 
-
<!--
+
==Crystal Structure of the Arabidopsis thaliana O-Acetyl-Serine-(Thiol)- Lyase C==
-
The line below this paragraph, containing "STRUCTURE_4aec", creates the "Structure Box" on the page.
+
<StructureSection load='4aec' size='340' side='right'caption='[[4aec]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<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>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</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>
-
{{STRUCTURE_4aec| PDB=4aec | SCENE= }}
+
<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.
-
===Crystal Structure of the Arabidopsis thaliana O-Acetyl-Serine-(Thiol)- Lyase C===
+
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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<!--
+
</div>
-
The line below this paragraph, {{ABSTRACT_PUBMED_22325778}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 4aec" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 22325778 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_22325778}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
-
[[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].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:022325778</ref><references group="xtra"/>
+
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
-
[[Category: Cysteine synthase]]
+
[[Category: Large Structures]]
-
[[Category: Feldman-Salit, A.]]
+
[[Category: Feldman-Salit A]]
-
[[Category: Hell, R.]]
+
[[Category: Hell R]]
-
[[Category: Hothorn, M.]]
+
[[Category: Hothorn M]]
-
[[Category: Lenherr, E D.]]
+
[[Category: Lenherr ED]]
-
[[Category: Scheffzek, K.]]
+
[[Category: Scheffzek K]]
-
[[Category: Throm, C.]]
+
[[Category: Throm C]]
-
[[Category: Wade, R C.]]
+
[[Category: Wade RC]]
-
[[Category: Wirtz, M.]]
+
[[Category: Wirtz M]]
-
[[Category: Assimilatory sulfate reduction]]
+
-
[[Category: Cysteine synthesis]]
+
-
[[Category: Lyase]]
+
-
[[Category: Plant inorganic sulfur uptake]]
+
-
[[Category: Sulfide]]
+

Current revision

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

PDB ID 4aec

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4aec"
Personal tools