2dtj: Difference between revisions

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[[Image:2dtj.png|left|200px]]


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==Crystal structure of regulatory subunit of aspartate kinase from Corynebacterium glutamicum==
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<StructureSection load='2dtj' size='340' side='right'caption='[[2dtj]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2dtj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_glutamicum Corynebacterium glutamicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DTJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DTJ FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.58&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=THR:THREONINE'>THR</scene></td></tr>
{{STRUCTURE_2dtj|  PDB=2dtj  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2dtj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dtj OCA], [https://pdbe.org/2dtj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dtj RCSB], [https://www.ebi.ac.uk/pdbsum/2dtj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dtj 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>
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    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dt/2dtj_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=2dtj ConSurf].
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== Publication Abstract from PubMed ==
Aspartate kinase (AK) catalyzes the first step of the biosynthesis of the aspartic acid family amino acids, and is regulated via feedback inhibition by end-products including Thr and Lys. To elucidate the mechanism of this inhibition, we determined the crystal structure of the regulatory subunit of AK from Corynebacterium glutamicum at 1.58 A resolution in the Thr-binding form, the first crystal structure of the regulatory subunit of alpha(2)beta(2)-type AK. The regulatory subunit contains two ACT domain motifs per monomer and is arranged as a dimer. Two non-equivalent ACT domains from different chains form an effector-binding unit that binds a single Thr molecule, and the resulting two effector-binding units of the dimer associate perpendicularly in a face-to-face manner. The regulatory subunit is a monomer in the absence of Thr but becomes a dimer by adding Thr. The dimerization is eliminated in mutant AKs with changes in the Thr-binding region, suggesting that the dimerization induced by Thr binding is a key step in the inhibitory mechanism of AK from C. glutamicum. A putative Lys-binding site and the inhibitory mechanism of CgAK are discussed.


===Crystal structure of regulatory subunit of aspartate kinase from Corynebacterium glutamicum===
Structural Insight into concerted inhibition of alpha 2 beta 2-type aspartate kinase from Corynebacterium glutamicum.,Yoshida A, Tomita T, Kurihara T, Fushinobu S, Kuzuyama T, Nishiyama M J Mol Biol. 2007 Apr 27;368(2):521-36. Epub 2007 Feb 20. PMID:17350037<ref>PMID:17350037</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
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<references/>
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</StructureSection>
==About this Structure==
2DTJ is a [[Single protein]] structure of 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=2DTJ OCA].
 
==Reference==
Structural Insight into concerted inhibition of alpha 2 beta 2-type aspartate kinase from Corynebacterium glutamicum., Yoshida A, Tomita T, Kurihara T, Fushinobu S, Kuzuyama T, Nishiyama M, J Mol Biol. 2007 Apr 27;368(2):521-36. Epub 2007 Feb 20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17350037 17350037]
 
Cloning of a DNA fragment from Corynebacterium glutamicum conferring aminoethyl cysteine resistance and feedback resistance to aspartokinase., Thierbach G, Kalinowski J, Bachmann B, Puhler A, Appl Microbiol Biotechnol. 1990 Jan;32(4):443-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1366393 1366393]
 
Genetic and biochemical analysis of the aspartokinase from Corynebacterium glutamicum., Kalinowski J, Cremer J, Bachmann B, Eggeling L, Sahm H, Puhler A, Mol Microbiol. 1991 May;5(5):1197-204. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1956296 1956296]
 
Conversion of feedback regulation in aspartate kinase by domain exchange., Kato C, Kurihara T, Kobashi N, Yamane H, Nishiyama M, Biochem Biophys Res Commun. 2004 Apr 9;316(3):802-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15033471 15033471]
[[Category: Aspartate kinase]]
[[Category: Corynebacterium glutamicum]]
[[Category: Corynebacterium glutamicum]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Fushinobu, S.]]
[[Category: Fushinobu S]]
[[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: Protein-ligand complex]]
[[Category: Regulatory subunit]]
 
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