3c1n: Difference between revisions

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New page: left|200px {{Structure |PDB= 3c1n |SIZE=350|CAPTION= <scene name='initialview01'>3c1n</scene>, resolution 2.720Å |SITE= <scene name='pdbsite=AC1:THR+Binding+Site...
 
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[[Image:3c1n.jpg|left|200px]]


{{Structure
==Crystal Structure of Allosteric Inhibition Threonine-sensitive Aspartokinase from Methanococcus jannaschii with L-threonine==
|PDB= 3c1n |SIZE=350|CAPTION= <scene name='initialview01'>3c1n</scene>, resolution 2.720&Aring;
<StructureSection load='3c1n' size='340' side='right'caption='[[3c1n]], [[Resolution|resolution]] 2.72&Aring;' scene=''>
|SITE= <scene name='pdbsite=AC1:THR+Binding+Site+For+Residue+A+470'>AC1</scene>, <scene name='pdbsite=AC2:THR+Binding+Site+For+Residue+A+471'>AC2</scene>, <scene name='pdbsite=AC3:THR+Binding+Site+For+Residue+A+472'>AC3</scene>, <scene name='pdbsite=AC4:THR+Binding+Site+For+Residue+A+473'>AC4</scene>, <scene name='pdbsite=AC5:THR+Binding+Site+For+Residue+A+474'>AC5</scene>, <scene name='pdbsite=AC6:THR+Binding+Site+For+Residue+A+475'>AC6</scene> and <scene name='pdbsite=AC7:THR+Binding+Site+For+Residue+A+476'>AC7</scene>
== Structural highlights ==
|LIGAND= <scene name='pdbligand=THR:THREONINE'>THR</scene>
<table><tr><td colspan='2'>[[3c1n]] 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=3C1N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C1N 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]] 2.72&#8491;</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=THR:THREONINE'>THR</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=3c1n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c1n OCA], [https://pdbe.org/3c1n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c1n RCSB], [https://www.ebi.ac.uk/pdbsum/3c1n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c1n ProSAT]</span></td></tr>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3c1n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c1n OCA], [http://www.ebi.ac.uk/pdbsum/3c1n PDBsum], [http://www.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=3c1n RCSB]</span>
</table>
}}
== Function ==
[https://www.uniprot.org/uniprot/AK_METJA AK_METJA]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c1/3c1n_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=3c1n ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


'''Crystal Structure of Allosteric Inhibition Threonine-sensitive Aspartokinase from Methanococcus jannaschii with L-threonine'''
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<ref>PMID:18334478</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
==Overview==
</div>
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.
<div class="pdbe-citations 3c1n" style="background-color:#fffaf0;"></div>
 
== References ==
==About this Structure==
<references/>
3C1N 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=3C1N OCA].
__TOC__
 
</StructureSection>
==Reference==
[[Category: Large Structures]]
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]
[[Category: Aspartate kinase]]
[[Category: Methanocaldococcus jannaschii]]
[[Category: Methanocaldococcus jannaschii]]
[[Category: Single protein]]
[[Category: Liu X]]
[[Category: Liu, X.]]
[[Category: Pavlovshy AG]]
[[Category: Pavlovshy, A G.]]
[[Category: Viola RE]]
[[Category: Viola, R E.]]
[[Category: act domain]]
[[Category: allosteric inhibition]]
[[Category: amino-acid biosynthesis]]
[[Category: kinase]]
[[Category: threonine biosynthesis]]
[[Category: threonine-sensitive]]
[[Category: transferase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 26 09:57:31 2008''

Latest revision as of 15:19, 30 August 2023

Crystal Structure of Allosteric Inhibition Threonine-sensitive Aspartokinase from Methanococcus jannaschii with L-threonineCrystal Structure of Allosteric Inhibition Threonine-sensitive Aspartokinase from Methanococcus jannaschii with L-threonine

Structural highlights

3c1n is a 4 chain structure with sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.72Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

  1. ↑ 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

3c1n, resolution 2.72Å

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