3c1m

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[[Image:3c1m.jpg|left|200px]]
[[Image:3c1m.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 3c1m |SIZE=350|CAPTION= <scene name='initialview01'>3c1m</scene>, resolution 2.30&Aring;
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The line below this paragraph, containing "STRUCTURE_3c1m", creates the "Structure Box" on the page.
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|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>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|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>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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or leave the SCENE parameter empty for the default display.
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|GENE= MJ0571 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 Methanocaldococcus jannaschii])
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-->
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|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>
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{{STRUCTURE_3c1m| PDB=3c1m | SCENE= }}
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|RELATEDENTRY=[[3c1n|3C1N]]
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|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>
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}}
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'''Cyrstal Structure of threonine-sensitive aspartokinase from Methanococcus jannaschii with MgAMP-PNP and L-aspartate'''
'''Cyrstal Structure of threonine-sensitive aspartokinase from Methanococcus jannaschii with MgAMP-PNP and L-aspartate'''
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Liu, X.]]
[[Category: Liu, X.]]
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[[Category: act domain]]
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[[Category: Act domain]]
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[[Category: allosteric inhibition]]
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[[Category: Allosteric inhibition]]
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[[Category: amino-acid biosynthesis]]
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[[Category: Amino-acid biosynthesis]]
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[[Category: kinase]]
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[[Category: Kinase]]
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[[Category: threonine biosynthesis]]
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[[Category: Threonine biosynthesis]]
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[[Category: threonine-sensitive]]
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[[Category: Threonine-sensitive]]
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[[Category: transferase]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 21:17:20 2008''
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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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Revision as of 18:17, 4 May 2008

Image:3c1m.jpg

Template:STRUCTURE 3c1m

Cyrstal Structure of threonine-sensitive aspartokinase from Methanococcus jannaschii with MgAMP-PNP and L-aspartate


Overview

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.

About this Structure

3C1M is a Single protein structure of sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA.

Reference

The structural basis for allosteric Inhibition of a threonine-sensitive aspartokinase., Liu X, Pavlovsky AG, Viola RE, J Biol Chem. 2008 Mar 11;. PMID:18334478 Page seeded by OCA on Sun May 4 21:17:20 2008

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