3aaw

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[[Image:3aaw.png|left|200px]]
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==Crystal structure of aspartate kinase from Corynebacterium glutamicum in complex with lysine and threonine==
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<StructureSection load='3aaw' size='340' side='right' caption='[[3aaw]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AAW FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LYS:LYSINE'>LYS</scene>, <scene name='pdbligand=THR:THREONINE'>THR</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ab4|3ab4]], [[3ab2|3ab2]], [[2dtj|2dtj]]</td></tr>
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<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]), lysC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=168810 Corynebacterium crenatum])</td></tr>
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<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>
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<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=3aaw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aaw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3aaw RCSB], [http://www.ebi.ac.uk/pdbsum/3aaw PDBsum]</span></td></tr>
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</table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/aa/3aaw_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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{{STRUCTURE_3aaw| PDB=3aaw | SCENE= }}
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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>
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===Crystal structure of aspartate kinase from Corynebacterium glutamicum in complex with lysine and threonine===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_20573952}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[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].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:020573952</ref><ref group="xtra">PMID:017350037</ref><references group="xtra"/>
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[[Category: Aspartate kinase]]
[[Category: Aspartate kinase]]
[[Category: Corynebacterium crenatum]]
[[Category: Corynebacterium crenatum]]
[[Category: Corynebacterium glutamicum]]
[[Category: Corynebacterium glutamicum]]
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[[Category: Kuzuyama, T.]]
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[[Category: Kuzuyama, T]]
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[[Category: Nishiyama, M.]]
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[[Category: Nishiyama, M]]
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[[Category: Tomita, T.]]
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[[Category: Tomita, T]]
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[[Category: Yoshida, A.]]
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[[Category: Yoshida, A]]
[[Category: Alternative initiation]]
[[Category: Alternative initiation]]
[[Category: Amino-acid biosynthesis]]
[[Category: Amino-acid biosynthesis]]
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[[Category: Aspartate kinase]]
 
[[Category: Atp-binding]]
[[Category: Atp-binding]]
[[Category: Concerted inhibition]]
[[Category: Concerted inhibition]]

Revision as of 08:10, 12 November 2014

Crystal structure of aspartate kinase from Corynebacterium glutamicum in complex with lysine and threonine

3aaw, resolution 2.50Å

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