2cdq: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:2cdq.png|left|200px]]
-<!--
+==Crystal structure of Arabidopsis thaliana aspartate kinase complexed with lysine and S- adenosylmethionine==
-The line below this paragraph, containing "STRUCTURE_2cdq", creates the "Structure Box" on the page.
+<StructureSection load='2cdq' size='340' side='right'caption='[[2cdq]], [[Resolution|resolution]] 2.85&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'>[[2cdq]] 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=2CDQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CDQ 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]] 2.85&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LYS:LYSINE'>LYS</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=TAR:D(-)-TARTARIC+ACID'>TAR</scene></td></tr>
-{{STRUCTURE_2cdq|  PDB=2cdq  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2cdq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cdq OCA], [https://pdbe.org/2cdq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cdq RCSB], [https://www.ebi.ac.uk/pdbsum/2cdq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cdq ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/AK1_ARATH AK1_ARATH] Involved in the first step of essential amino acids lysine, threonine, methionine and isoleucine synthesis via the aspartate-family pathway.
+== 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/cd/2cdq_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2cdq ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Asp kinase catalyzes the first step of the Asp-derived essential amino acid pathway in plants and microorganisms. Depending on the source organism, this enzyme contains up to four regulatory ACT domains and exhibits several isoforms under the control of a great variety of allosteric effectors. We report here the dimeric structure of a Lys and S-adenosylmethionine-sensitive Asp kinase isoform from Arabidopsis thaliana in complex with its two inhibitors. This work reveals the structure of an Asp kinase and an enzyme containing two ACT domains cocrystallized with its effectors. Only one ACT domain (ACT1) is implicated in effector binding. A loop involved in the binding of Lys and S-adenosylmethionine provides an explanation for the synergistic inhibition by these effectors. The presence of S-adenosylmethionine in the regulatory domain indicates that ACT domains are also able to bind nucleotides. The organization of ACT domains in the present structure is different from that observed in Thr deaminase and in the regulatory subunit of acetohydroxyacid synthase III.
-===CRYSTAL STRUCTURE OF ARABIDOPSIS THALIANA ASPARTATE KINASE COMPLEXED WITH LYSINE AND S-ADENOSYLMETHIONINE===
+A novel organization of ACT domains in allosteric enzymes revealed by the crystal structure of Arabidopsis aspartate kinase.,Mas-Droux C, Curien G, Robert-Genthon M, Laurencin M, Ferrer JL, Dumas R Plant Cell. 2006 Jul;18(7):1681-92. Epub 2006 May 26. PMID:16731588<ref>PMID:16731588</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_16731588}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 2cdq" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 16731588 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_16731588}}
+__TOC__
+</StructureSection>
-==About this Structure==
-CDQ is a [[Single protein]] 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=2CDQ OCA].
-==Reference==
-A novel organization of ACT domains in allosteric enzymes revealed by the crystal structure of Arabidopsis aspartate kinase., Mas-Droux C, Curien G, Robert-Genthon M, Laurencin M, Ferrer JL, Dumas R, Plant Cell. 2006 Jul;18(7):1681-92. Epub 2006 May 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16731588 16731588]
 [[Category: Arabidopsis thaliana]]
-[[Category: Aspartate kinase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Curien G]]
-[[Category: Curien, G.]]
+[[Category: Dumas R]]
-[[Category: Dumas, R.]]
+[[Category: Ferrer JL]]
-[[Category: Ferrer, J L.]]
+[[Category: Laurencin M]]
-[[Category: Laurencin, M.]]
+[[Category: Mas-Droux C]]
-[[Category: Mas-Droux, C.]]
+[[Category: Robert-Genthon M]]
-[[Category: Robert-Genthon, M.]]
-[[Category: Act domain]]
-[[Category: Allosteric effector]]
-[[Category: Allostery]]
-[[Category: Amino acid biosynthesis]]
-[[Category: Amino acid metabolism]]
-[[Category: Aspartate kinase]]
-[[Category: Lysine]]
-[[Category: Plant]]
-[[Category: S-adenosylmethionine]]
-[[Category: Transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:51:53 2008''