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[[Image:3aaw.png|left|200px]]


{{STRUCTURE_3aaw| PDB=3aaw | SCENE= }}
==Crystal structure of aspartate kinase from Corynebacterium glutamicum in complex with lysine and threonine==
<StructureSection load='3aaw' size='340' side='right'caption='[[3aaw]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3aaw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_crenatum Corynebacterium crenatum] and [https://en.wikipedia.org/wiki/Corynebacterium_glutamicum Corynebacterium glutamicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AAW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AAW 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]] 2.5&#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=THR:THREONINE'>THR</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=3aaw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aaw OCA], [https://pdbe.org/3aaw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aaw RCSB], [https://www.ebi.ac.uk/pdbsum/3aaw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aaw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AK_CORGL AK_CORGL] Catalyzes the phosphorylation of the beta-carboxyl group of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is involved in the branched biosynthetic pathway leading to the biosynthesis of amino acids lysine, threonine, isoleucine and methionine.<ref>PMID:17350037</ref> <ref>PMID:20573952</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/aa/3aaw_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=3aaw ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Aspartate kinase (AK) is the first and committed enzyme of the biosynthetic pathway producing aspartate family amino acids, lysine, threonine, and methionine. AK from Corynebacterium glutamicum (CgAK), a bacterium used for industrial fermentation of amino acids, including glutamate and lysine, is inhibited by lysine and threonine in a concerted manner. To elucidate the mechanism of this unique regulation in CgAK, we determined the crystal structures in several forms: an inhibitory form complexed with both lysine and threonine, an active form complexed with only threonine, and a feedback inhibition-resistant mutant (S301F) complexed with both lysine and threonine. CgAK has a characteristic alpha(2)beta(2)-type heterotetrameric structure made up of two alpha subunits and two beta subunits. Comparison of the crystal structures between inhibitory and active forms revealed that binding inhibitors causes a conformational change to a closed inhibitory form, and the interaction between the catalytic domain in the alpha subunit and beta subunit (regulatory subunit) is a key event for stabilizing the inhibitory form. This study shows not only the first crystal structures of alpha(2)beta(2)-type AK but also the mechanism of concerted inhibition in CgAK.


===Crystal structure of aspartate kinase from Corynebacterium glutamicum in complex with lysine and threonine===
Mechanism of concerted inhibition of alpha2beta2-type hetero-oligomeric aspartate kinase from Corynebacterium glutamicum.,Yoshida A, Tomita T, Kuzuyama T, Nishiyama M J Biol Chem. 2010 Aug 27;285(35):27477-86. Epub 2010 Jun 23. PMID:20573952<ref>PMID:20573952</ref>


{{ABSTRACT_PUBMED_20573952}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
==About this Structure==
<div class="pdbe-citations 3aaw" style="background-color:#fffaf0;"></div>
[[3aaw]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Corynebacterium_crenatum Corynebacterium crenatum] and [http://en.wikipedia.org/wiki/Corynebacterium_glutamicum Corynebacterium glutamicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AAW OCA].
== References ==
 
<references/>
==Reference==
__TOC__
<ref group="xtra">PMID:020573952</ref><ref group="xtra">PMID:017350037</ref><references group="xtra"/>
</StructureSection>
[[Category: Aspartate kinase]]
[[Category: Corynebacterium crenatum]]
[[Category: Corynebacterium crenatum]]
[[Category: Corynebacterium glutamicum]]
[[Category: Corynebacterium glutamicum]]
[[Category: Kuzuyama, T.]]
[[Category: Large Structures]]
[[Category: Nishiyama, M.]]
[[Category: Kuzuyama T]]
[[Category: Tomita, T.]]
[[Category: Nishiyama M]]
[[Category: Yoshida, A.]]
[[Category: Tomita T]]
[[Category: Alternative initiation]]
[[Category: Yoshida A]]
[[Category: Amino-acid biosynthesis]]
[[Category: Aspartate kinase]]
[[Category: Atp-binding]]
[[Category: Concerted inhibition]]
[[Category: Diaminopimelate biosynthesis]]
[[Category: Kinase]]
[[Category: Lysine biosynthesis]]
[[Category: Nucleotide-binding]]
[[Category: Transferase]]
Retrieved from "https://proteopedia.org/3aaw"