3e9y

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:03, 30 October 2024) (edit) (undo)
 
(10 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:3e9y.jpg|left|200px]]
 
-
<!--
+
==Arabidopsis thaliana acetohydroxyacid synthase in complex with monosulfuron==
-
The line below this paragraph, containing "STRUCTURE_3e9y", creates the "Structure Box" on the page.
+
<StructureSection load='3e9y' size='340' side='right'caption='[[3e9y]], [[Resolution|resolution]] 3.00&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'>[[3e9y]] is a 1 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=3E9Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E9Y 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]] 3&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1MS:N-[(4-METHYLPYRIMIDIN-2-YL)CARBAMOYL]-2-NITROBENZENESULFONAMIDE'>1MS</scene>, <scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=FAB:FLAVIN-ADENINE+DINUCLEOTIDE-N5-ISOBUTYL+KETONE'>FAB</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</scene>, <scene name='pdbligand=TDM:2-[(2E)-3-[(4-AMINO-2-METHYLPYRIMIDIN-5-YL)METHYL]-2-(1-HYDROXYETHYLIDENE)-4-METHYL-2,3-DIHYDRO-1,3-THIAZOL-5-YL]ETHYL+TRIHYDROGEN+DIPHOSPHATE'>TDM</scene></td></tr>
-
{{STRUCTURE_3e9y| PDB=3e9y | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3e9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e9y OCA], [https://pdbe.org/3e9y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e9y RCSB], [https://www.ebi.ac.uk/pdbsum/3e9y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e9y ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/ILVB_ARATH ILVB_ARATH] Catalyzes the formation of acetolactate from pyruvate, the first step in valine and isoleucine biosynthesis.<ref>PMID:16665813</ref> <ref>PMID:2336405</ref> [:]<ref>PMID:16667374</ref> <ref>PMID:16668488</ref> <ref>PMID:8913312</ref> <ref>PMID:9355748</ref> <ref>PMID:9677339</ref> <ref>PMID:10386618</ref>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e9/3e9y_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3e9y ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Acetohydroxyacid synthase (AHAS; EC 2.2.1.6) is the first enzyme in the biosynthetic pathway of the branched-chain amino acids. It catalyzes the conversion of two molecules of pyruvate into 2-acetolactate or one molecule of pyruvate and one molecule of 2-ketobutyrate into 2-aceto-2-hydroxybutyrate. AHAS requires the cofactors thiamine diphosphate (ThDP), Mg(2+) and FAD for activity. The herbicides that target this enzyme are effective in protecting a broad range of crops from weed species. However, resistance in the field is now a serious problem worldwide. To address this, two new sulfonylureas, monosulfuron and monosulfuron ester, have been developed as commercial herbicides in China. These molecules differ from the traditional sulfonylureas in that the heterocyclic ring attached to the nitrogen atom of the sulfonylurea bridge is monosubstituted rather than disubstituted. The structures of these compounds in complex with the catalytic subunit of Arabidopsis thaliana AHAS have been determined to 3.0 and 2.8 A, respectively. In both complexes, these molecules are bound in the tunnel leading to the active site, such that the sole substituent of the heterocyclic ring is buried deepest and oriented towards the ThDP. Unlike the structures of Arabidopsis thaliana AHAS in complex with the classic disubstituted sulfonylureas, where ThDP is broken, this cofactor is intact and present most likely as the hydroxylethyl intermediate.
-
===Arabidopsis thaliana acetohydroxyacid synthase in complex with monosulfuron===
+
Crystal structures of two novel sulfonylurea herbicides in complex with Arabidopsis thaliana acetohydroxyacid synthase.,Wang JG, Lee PK, Dong YH, Pang SS, Duggleby RG, Li ZM, Guddat LW FEBS J. 2009 Mar;276(5):1282-90. PMID:19187232<ref>PMID:19187232</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_19187232}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 3e9y" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 19187232 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_19187232}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
-
3E9Y is a 1 chain structure of 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=3E9Y OCA].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:19187232</ref><references group="xtra"/>
+
-
[[Category: Acetolactate synthase]]
+
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
-
[[Category: Duggleby, R G.]]
+
[[Category: Large Structures]]
-
[[Category: Guddat, L W.]]
+
[[Category: Duggleby RG]]
-
[[Category: Li, Z M.]]
+
[[Category: Guddat LW]]
-
[[Category: Wang, J G.]]
+
[[Category: Li Z-M]]
-
[[Category: Amino-acid biosynthesis]]
+
[[Category: Wang J-G]]
-
[[Category: Branched-chain amino acid biosynthesis]]
+
-
[[Category: Chloroplast]]
+
-
[[Category: Fad]]
+
-
[[Category: Flavoprotein]]
+
-
[[Category: Genetically modified food]]
+
-
[[Category: Herbicide resistance]]
+
-
[[Category: Magnesium]]
+
-
[[Category: Metal-binding]]
+
-
[[Category: Plastid]]
+
-
[[Category: Protein-fad-hethdp complex]]
+
-
[[Category: Thiamine pyrophosphate]]
+
-
[[Category: Transferase]]
+
-
[[Category: Transit peptide]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 2 15:29:28 2009''
+

Current revision

Arabidopsis thaliana acetohydroxyacid synthase in complex with monosulfuron

PDB ID 3e9y

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/3e9y"
Personal tools