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| | <StructureSection load='3c20' size='340' side='right'caption='[[3c20]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='3c20' size='340' side='right'caption='[[3c20]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3c20]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C20 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C20 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3c20]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C20 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C20 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3c1m|3c1m]], [[3c1n|3c1n]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MJ0571 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 ATCC 43067])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Aspartate_kinase Aspartate kinase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3c20 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c20 OCA], [https://pdbe.org/3c20 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c20 RCSB], [https://www.ebi.ac.uk/pdbsum/3c20 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c20 ProSAT]</span></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=3c20 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c20 OCA], [https://pdbe.org/3c20 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c20 RCSB], [https://www.ebi.ac.uk/pdbsum/3c20 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c20 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/AK_METJA AK_METJA] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aspartate kinase]] | |
| - | [[Category: Atcc 43067]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Liu, X]] | + | [[Category: Methanocaldococcus jannaschii]] |
| - | [[Category: Pavlovsky, A G]] | + | [[Category: Liu X]] |
| - | [[Category: Viola, R E]] | + | [[Category: Pavlovsky AG]] |
| - | [[Category: Act domain]] | + | [[Category: Viola RE]] |
| - | [[Category: Allosetric inhibition]]
| + | |
| - | [[Category: Amino-acid biosynthesis]]
| + | |
| - | [[Category: Kinase]]
| + | |
| - | [[Category: Theronine-sensitive]]
| + | |
| - | [[Category: Threonine biosynthesis]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
AK_METJA
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The commitment step to the aspartate pathway of amino acid biosynthesis is the phosphorylation of aspartic acid catalyzed by aspartokinase (AK). Most microorganisms and plants have multiple forms of this enzyme, and many of these isofunctional enzymes are subject to feedback regulation by the end products of the pathway. However, the archeal species Methanococcus jannaschii has only a single, monofunctional form of AK. The substrate l-aspartate binds to this recombinant enzyme in two different orientations, providing the first structural evidence supporting the relaxed regiospecificity previously observed with several alternative substrates of Escherichia coli AK ( Angeles, T. S., Hunsley, J. R., and Viola, R. E. (1992) Biochemistry 31, 799-805 ). Binding of the nucleotide substrate triggers significant domain movements that result in a more compact quaternary structure. In contrast, the highly cooperative binding of the allosteric regulator l-threonine to multiple sites on this dimer of dimers leads to an open enzyme structure. A comparison of these structures supports a mechanism for allosteric regulation in which the domain movements induced by threonine binding causes displacement of the substrates from the enzyme, resulting in a relaxed, inactive conformation.
The structural basis for allosteric inhibition of a threonine-sensitive aspartokinase.,Liu X, Pavlovsky AG, Viola RE J Biol Chem. 2008 Jun 6;283(23):16216-25. Epub 2008 Mar 11. PMID:18334478[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Liu X, Pavlovsky AG, Viola RE. The structural basis for allosteric inhibition of a threonine-sensitive aspartokinase. J Biol Chem. 2008 Jun 6;283(23):16216-25. Epub 2008 Mar 11. PMID:18334478 doi:10.1074/jbc.M800760200
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