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| | <StructureSection load='2j0w' size='340' side='right'caption='[[2j0w]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='2j0w' size='340' side='right'caption='[[2j0w]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2j0w]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J0W OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2J0W FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2j0w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J0W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J0W FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ohi|1ohi]], [[2j0x|2j0x]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=2j0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j0w OCA], [https://pdbe.org/2j0w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j0w RCSB], [https://www.ebi.ac.uk/pdbsum/2j0w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j0w ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2j0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j0w OCA], [http://pdbe.org/2j0w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2j0w RCSB], [http://www.ebi.ac.uk/pdbsum/2j0w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2j0w ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/AK3_ECOLI AK3_ECOLI] |
| | == 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: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| - | [[Category: Aspartate kinase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hawkins, A R]] | + | [[Category: Hawkins AR]] |
| - | [[Category: Kotaka, M]] | + | [[Category: Kotaka M]] |
| - | [[Category: Lockyer, M]] | + | [[Category: Lockyer M]] |
| - | [[Category: Ren, J]] | + | [[Category: Ren J]] |
| - | [[Category: Stammers, D K]] | + | [[Category: Stammers DK]] |
| - | [[Category: Act domain]]
| + | |
| - | [[Category: Allosteric regulation]]
| + | |
| - | [[Category: Amino acid biosynthesis]]
| + | |
| - | [[Category: Amino-acid biosynthesis]]
| + | |
| - | [[Category: Aspartate pathway]]
| + | |
| - | [[Category: Aspartokinase]]
| + | |
| - | [[Category: Feedback inhibition]]
| + | |
| - | [[Category: Kinase]]
| + | |
| - | [[Category: Lysine biosynthesis]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
AK3_ECOLI
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
Aspartokinase III (AKIII) from Escherichia coli catalyzes an initial commitment step of the aspartate pathway, giving biosynthesis of certain amino acids including lysine. We report crystal structures of AKIII in the inactive T-state with bound feedback allosteric inhibitor lysine and in the R-state with aspartate and ADP. The structures reveal an unusual configuration for the regulatory ACT domains, in which ACT2 is inserted into ACT1 rather than the expected tandem repeat. Comparison of R- and T-state AKIII indicates that binding of lysine to the regulatory ACT1 domain in R-state AKIII instigates a series of changes that release a "latch", the beta15-alphaK loop, from the catalytic domain, which in turn undergoes large rotational rearrangements, promoting tetramer formation and completion of the transition to the T-state. Lysine-induced allosteric transition in AKIII involves both destabilizing the R-state and stabilizing the T-state tetramer. Rearrangement of the catalytic domain blocks the ATP-binding site, which is therefore the structural basis for allosteric inhibition of AKIII by lysine.
Structures of R- and T-state Escherichia coli aspartokinase III. Mechanisms of the allosteric transition and inhibition by lysine.,Kotaka M, Ren J, Lockyer M, Hawkins AR, Stammers DK J Biol Chem. 2006 Oct 20;281(42):31544-52. Epub 2006 Aug 12. PMID:16905770[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kotaka M, Ren J, Lockyer M, Hawkins AR, Stammers DK. Structures of R- and T-state Escherichia coli aspartokinase III. Mechanisms of the allosteric transition and inhibition by lysine. J Biol Chem. 2006 Oct 20;281(42):31544-52. Epub 2006 Aug 12. PMID:16905770 doi:10.1074/jbc.M605886200
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