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| [[Image:3c1m.jpg|left|200px]]
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| {{Structure
| | ==Cyrstal Structure of threonine-sensitive aspartokinase from Methanococcus jannaschii with MgAMP-PNP and L-aspartate== |
| |PDB= 3c1m |SIZE=350|CAPTION= <scene name='initialview01'>3c1m</scene>, resolution 2.30Å
| | <StructureSection load='3c1m' size='340' side='right'caption='[[3c1m]], [[Resolution|resolution]] 2.30Å' scene=''> |
| |SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Residue+A+1'>AC1</scene>, <scene name='pdbsite=AC2:Mg+Binding+Site+For+Residue+B+471'>AC2</scene>, <scene name='pdbsite=AC3:Mg+Binding+Site+For+Residue+C+471'>AC3</scene>, <scene name='pdbsite=AC4:Mg+Binding+Site+For+Residue+D+471'>AC4</scene>, <scene name='pdbsite=AC5:ASP+Binding+Site+For+Residue+B+472'>AC5</scene>, <scene name='pdbsite=AC6:ASP+Binding+Site+For+Residue+B+473'>AC6</scene>, <scene name='pdbsite=AC7:ASP+Binding+Site+For+Residue+B+474'>AC7</scene>, <scene name='pdbsite=AC8:ASP+Binding+Site+For+Residue+B+475'>AC8</scene>, <scene name='pdbsite=AC9:Anp+Binding+Site+For+Residue+A+471'>AC9</scene>, <scene name='pdbsite=BC1:Anp+Binding+Site+For+Residue+B+476'>BC1</scene>, <scene name='pdbsite=BC2:Anp+Binding+Site+For+Residue+C+472'>BC2</scene>, <scene name='pdbsite=BC3:Anp+Binding+Site+For+Residue+D+472'>BC3</scene>, <scene name='pdbsite=BC4:Fmt+Binding+Site+For+Residue+A+472'>BC4</scene>, <scene name='pdbsite=BC5:Fmt+Binding+Site+For+Residue+A+475'>BC5</scene>, <scene name='pdbsite=BC6:Fmt+Binding+Site+For+Residue+C+473'>BC6</scene> and <scene name='pdbsite=BC7:Fmt+Binding+Site+For+Residue+D+473'>BC7</scene>
| | == Structural highlights == |
| |LIGAND= <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
| | <table><tr><td colspan='2'>[[3c1m]] is a 4 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=3C1M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C1M FirstGlance]. <br> |
| |ACTIVITY= <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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| |GENE= MJ0571 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 Methanocaldococcus jannaschii])
| | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=ASP:ASPARTIC+ACID'>ASP</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| |DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd04921 ACT_AKi-HSDH-ThrA-like_1], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=PRK06291 PRK06291], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd04892 ACT_AK-like_2], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd04244 AAK_AK-LysC-like]</span>
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3c1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c1m OCA], [https://pdbe.org/3c1m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c1m RCSB], [https://www.ebi.ac.uk/pdbsum/3c1m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c1m ProSAT]</span></td></tr> |
| |RELATEDENTRY=[[3c1n|3C1N]]
| | </table> |
| |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3c1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c1m OCA], [http://www.ebi.ac.uk/pdbsum/3c1m PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3c1m RCSB]</span>
| | == Function == |
| }}
| | [https://www.uniprot.org/uniprot/AK_METJA AK_METJA] |
| | | == Evolutionary Conservation == |
| '''Cyrstal Structure of threonine-sensitive aspartokinase from Methanococcus jannaschii with MgAMP-PNP and L-aspartate'''
| | [[Image:Consurf_key_small.gif|200px|right]] |
| | | Check<jmol> |
| | | <jmolCheckbox> |
| ==Overview== | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c1/3c1m_consurf.spt"</scriptWhenChecked> |
| 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 M. 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 E. coli AK (Angeles et al., Biochemistry 31, 799, 1992). 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 a more open enzyme structure. A comparison of these structures supports a mechanism for allosteric regulation of AK in which the domain movements induced by threonine binding causes displacement of the substrates from the enzyme resulting in a relaxed, inactive conformation.
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | | <text>to colour the structure by Evolutionary Conservation</text> |
| ==About this Structure== | | </jmolCheckbox> |
| 3C1M is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C1M OCA].
| | </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=3c1m ConSurf]. |
| | | <div style="clear:both"></div> |
| ==Reference== | | __TOC__ |
| The structural basis for allosteric Inhibition of a threonine-sensitive aspartokinase., Liu X, Pavlovsky AG, Viola RE, J Biol Chem. 2008 Mar 11;. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18334478 18334478]
| | </StructureSection> |
| [[Category: Aspartate kinase]] | | [[Category: Large Structures]] |
| [[Category: Methanocaldococcus jannaschii]] | | [[Category: Methanocaldococcus jannaschii]] |
| [[Category: Single protein]]
| | [[Category: Liu X]] |
| [[Category: Liu, X.]] | |
| [[Category: act domain]]
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| [[Category: allosteric inhibition]]
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| [[Category: amino-acid biosynthesis]]
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| [[Category: kinase]]
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| [[Category: threonine biosynthesis]]
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| [[Category: threonine-sensitive]]
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| [[Category: transferase]]
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| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:30:10 2008''
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