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==Crystal structure of the regulatory subunit of aspartate kinase from Thermus flavus==
The line below this paragraph, containing "STRUCTURE_2dt9", creates the "Structure Box" on the page.
<StructureSection load='2dt9' size='340' side='right'caption='[[2dt9]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2dt9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DT9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DT9 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]] 2.15&#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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=THR:THREONINE'>THR</scene></td></tr>
{{STRUCTURE_2dt9|  PDB=2dt9  |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2dt9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dt9 OCA], [https://pdbe.org/2dt9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dt9 RCSB], [https://www.ebi.ac.uk/pdbsum/2dt9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dt9 ProSAT]</span></td></tr>
 
</table>
'''Crystal structure of the regulatory subunit of aspartate kinase from Thermus flavus'''
== Function ==
 
[https://www.uniprot.org/uniprot/AK_THETH AK_THETH] Catalyzes the phosphorylation of the beta-carboxyl group of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is involved in the branched biosynthetic pathway leading to the biosynthesis of amino acids threonine, isoleucine and methionine.<ref>PMID:7773416</ref> <ref>PMID:16232547</ref>
 
== Evolutionary Conservation ==
==Overview==
[[Image:Consurf_key_small.gif|200px|right]]
To reveal the catalytic mechanism of Thermus aspartate kinase, each of 29 amino acid residues that were highly conserved in the sequenced aspartate kinases, was replaced with alanine or leucine by PCR site-directed mutagenesis. Comparison of the kinetic parameters of these mutants with those of the wild-type aspartate kinase suggested that Thr47 was involved in binding aspartate and that Lys7 and Glu74 were involved in catalysis. Analysis of the effective concentrations of magnesium ion on the activity showed that the mutants with replacements at Ser41, Thr47, Asp154 and Asp182 required higher concentrations of magnesium ion. This suggests that these four residues play important roles in the binding of magnesium ions which are required for enzymatic activity.
Check<jmol>
 
  <jmolCheckbox>
==About this Structure==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dt/2dt9_consurf.spt"</scriptWhenChecked>
2DT9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DT9 OCA].  
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==Reference==
  </jmolCheckbox>
Kinetic and mutation analyses of aspartate kinase from Thermus flavus., Kobashi N, Nishiyama M, Tanokura M, J Biosci Bioeng. 1999;87(6):739-45. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16232547 16232547]
</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=2dt9 ConSurf].
[[Category: Aspartate kinase]]
<div style="clear:both"></div>
[[Category: Single protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
[[Category: Fushinobu, S.]]
[[Category: Fushinobu S]]
[[Category: Kuzuyama, T.]]
[[Category: Kuzuyama T]]
[[Category: Nishiyama, M.]]
[[Category: Nishiyama M]]
[[Category: Tomita, T.]]
[[Category: Tomita T]]
[[Category: Yoshida, A.]]
[[Category: Yoshida A]]
[[Category: Protein-ligand complex]]
[[Category: Regulatory subunit]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 01:18:29 2008''

Latest revision as of 16:48, 13 March 2024

Crystal structure of the regulatory subunit of aspartate kinase from Thermus flavusCrystal structure of the regulatory subunit of aspartate kinase from Thermus flavus

Structural highlights

2dt9 is a 2 chain structure with sequence from Thermus thermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.15Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AK_THETH Catalyzes the phosphorylation of the beta-carboxyl group of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is involved in the branched biosynthetic pathway leading to the biosynthesis of amino acids threonine, isoleucine and methionine.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ Nishiyama M, Kukimoto M, Beppu T, Horinouchi S. An operon encoding aspartokinase and purine phosphoribosyltransferase in Thermus flavus. Microbiology. 1995 May;141 ( Pt 5):1211-9. PMID:7773416
  2. ↑ Kobashi N, Nishiyama M, Tanokura M. Kinetic and mutation analyses of aspartate kinase from Thermus flavus. J Biosci Bioeng. 1999;87(6):739-45. PMID:16232547

2dt9, resolution 2.15Å

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