2dtj

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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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The line below this paragraph, containing "STRUCTURE_2dtj", creates the "Structure Box" on the page.
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<StructureSection load='2dtj' size='340' side='right'caption='[[2dtj]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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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>
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{{STRUCTURE_2dtj| PDB=2dtj | SCENE= }}
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<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>
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</table>
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== Function ==
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[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>
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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/dt/2dtj_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/main_output.php?pdb_ID=2dtj 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) 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.
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===Crystal structure of regulatory subunit of aspartate kinase from Corynebacterium glutamicum===
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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>
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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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The line below this paragraph, {{ABSTRACT_PUBMED_17350037}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2dtj" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 17350037 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17350037}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[2dtj]] is a 2 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=2DTJ OCA].
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==Reference==
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<ref group="xtra">PMID:17350037</ref><ref group="xtra">PMID:1366393</ref><ref group="xtra">PMID:1956296</ref><ref group="xtra">PMID:15033471</ref><references group="xtra"/>
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[[Category: Aspartate kinase]]
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[[Category: Corynebacterium glutamicum]]
[[Category: Corynebacterium glutamicum]]
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[[Category: Fushinobu, S.]]
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[[Category: Large Structures]]
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[[Category: Kuzuyama, T.]]
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[[Category: Fushinobu S]]
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[[Category: Nishiyama, M.]]
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[[Category: Kuzuyama T]]
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[[Category: Tomita, T.]]
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[[Category: Nishiyama M]]
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[[Category: Yoshida, A.]]
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[[Category: Tomita T]]
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[[Category: Protein-ligand complex]]
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[[Category: Yoshida A]]
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[[Category: Regulatory subunit]]
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[[Category: Transferase]]
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Current revision

Crystal structure of regulatory subunit of aspartate kinase from Corynebacterium glutamicum

PDB ID 2dtj

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