2cdq: Difference between revisions
New page: left|200px<br /> <applet load="2cdq" size="450" color="white" frame="true" align="right" spinBox="true" caption="2cdq, resolution 2.85Å" /> '''CRYSTAL STRUCTURE O... |
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== | ==Crystal structure of Arabidopsis thaliana aspartate kinase complexed with lysine and S- adenosylmethionine== | ||
Asp kinase catalyzes the first step of the Asp-derived essential amino | <StructureSection load='2cdq' size='340' side='right'caption='[[2cdq]], [[Resolution|resolution]] 2.85Å' scene=''> | ||
== Structural highlights == | |||
<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> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.85Å</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> | |||
<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. | |||
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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2cdq" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Arabidopsis thaliana]] | [[Category: Arabidopsis thaliana]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Curien | [[Category: Curien G]] | ||
[[Category: Dumas | [[Category: Dumas R]] | ||
[[Category: Ferrer | [[Category: Ferrer JL]] | ||
[[Category: Laurencin | [[Category: Laurencin M]] | ||
[[Category: Mas-Droux | [[Category: Mas-Droux C]] | ||
[[Category: Robert-Genthon | [[Category: Robert-Genthon M]] | ||
