3c20: Difference between revisions

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==Crystal Structure of Threonine-sensitive Aspartokinase from Methanococcus jannaschii with L-aspartate==
The line below this paragraph, containing "STRUCTURE_3c20", creates the "Structure Box" on the page.
<StructureSection load='3c20' size='340' side='right'caption='[[3c20]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#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=ASP:ASPARTIC+ACID'>ASP</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></td></tr>
{{STRUCTURE_3c20|  PDB=3c20  |  SCENE=  }}
<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>
== 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/c2/3c20_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=3c20 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 Threonine-sensitive Aspartokinase from Methanococcus jannaschii with L-aspartate'''
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 3c20" style="background-color:#fffaf0;"></div>
 
== References ==
==About this Structure==
<references/>
3C20 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=3C20 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: Pavlovsky AG]]
[[Category: Pavlovsky, A G.]]
[[Category: Viola RE]]
[[Category: Viola, R E.]]
[[Category: Act domain]]
[[Category: Allosetric inhibition]]
[[Category: Amino-acid biosynthesis]]
[[Category: Kinase]]
[[Category: Theronine-sensitive]]
[[Category: Threonine biosynthesis]]
[[Category: Transferase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 30 13:35:16 2008''

Latest revision as of 15:20, 30 August 2023

Crystal Structure of Threonine-sensitive Aspartokinase from Methanococcus jannaschii with L-aspartateCrystal Structure of Threonine-sensitive Aspartokinase from Methanococcus jannaschii with L-aspartate

Structural highlights

3c20 is a 2 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 2.7Å
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

3c20, resolution 2.70Å

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