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[[Image:3ab2.png|left|200px]]
==Crystal structure of aspartate kinase from Corynebacterium glutamicum in complex with threonine==
<StructureSection load='3ab2' size='340' side='right' caption='[[3ab2]], [[Resolution|resolution]] 2.59&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3ab2]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Corynebacterium_glutamicum Corynebacterium glutamicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AB2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AB2 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=THR:THREONINE'>THR</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ab4|3ab4]], [[3aaw|3aaw]], [[2dtj|2dtj]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lysC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1718 Corynebacterium glutamicum])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_kinase Aspartate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.4 2.7.2.4] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ab2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ab2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ab2 RCSB], [http://www.ebi.ac.uk/pdbsum/3ab2 PDBsum]</span></td></tr>
</table>
== 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/ab/3ab2_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/chain_selection.php?pdb_ID=2ata 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.


{{STRUCTURE_3ab2|  PDB=3ab2  |  SCENE=  }}
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>


===Crystal structure of aspartate kinase from Corynebacterium glutamicum in complex with threonine===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_20573952}}
== References ==
 
<references/>
==About this Structure==
__TOC__
[[3ab2]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Corynebacterium_glutamicum Corynebacterium glutamicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AB2 OCA].
</StructureSection>
 
==Reference==
<ref group="xtra">PMID:020573952</ref><ref group="xtra">PMID:017350037</ref><references group="xtra"/>
[[Category: Aspartate kinase]]
[[Category: Aspartate kinase]]
[[Category: Corynebacterium glutamicum]]
[[Category: Corynebacterium glutamicum]]
[[Category: Kuzuyama, T.]]
[[Category: Kuzuyama, T]]
[[Category: Nishiyama, M.]]
[[Category: Nishiyama, M]]
[[Category: Tomita, T.]]
[[Category: Tomita, T]]
[[Category: Yoshida, A.]]
[[Category: Yoshida, A]]
[[Category: Alternative initiation]]
[[Category: Alternative initiation]]
[[Category: Amino-acid biosynthesis]]
[[Category: Amino-acid biosynthesis]]
[[Category: Aspartate kinase]]
[[Category: Atp-binding]]
[[Category: Atp-binding]]
[[Category: Concerted inhibition]]
[[Category: Concerted inhibition]]
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