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==Crystal structure of the regulatory subunit of aspartate kinase from Thermus flavus==
==Crystal structure of the regulatory subunit of aspartate kinase from Thermus flavus==
<StructureSection load='2dt9' size='340' side='right' caption='[[2dt9]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
<StructureSection load='2dt9' size='340' side='right'caption='[[2dt9]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2dt9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DT9 FirstGlance]. <br>
<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>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=THR:THREONINE'>THR</scene></td></tr>
</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>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2dtj|2dtj]]</td></tr>
<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>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">askB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 "Flavobacterium thermophilum" Yoshida and Oshima 1971])</td></tr>
<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>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2dt9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dt9 OCA], [http://pdbe.org/2dt9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2dt9 RCSB], [http://www.ebi.ac.uk/pdbsum/2dt9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2dt9 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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>
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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].
</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].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Crystal structures of the regulatory subunit of Thr-sensitive aspartate kinase (AK; EC 2.7.2.4) from Thermus thermophilus (TtAKbeta) were determined at 2.15 A in the Thr-bound form (TtAKbeta-Thr) and at 2.98 A in the Thr-free form (TtAKbeta-free). Although both forms are crystallized as dimers, the contact surface area of the dimer interface in TtAKbeta-free (3200 A(2)) is smaller than that of TtAKbeta-Thr (3890 A(2)). Sedimentation equilibrium analyzed by ultracentrifugation revealed that TtAKbeta is present in equilibrium between a monomer and dimer, and that Thr binding shifts the equilibrium to dimer formation. In the absence of Thr, an outward shift of beta-strands near the Thr-binding site (site 1) and a concomitant loss of the electron density of the loop region between beta3 and beta4 near the Thr-binding site are observed. The mechanism of regulation by Thr is discussed on the basis of the crystal structures. TtAKbeta has higher thermostability than the regulatory subunit of Corynebacterium glutamicum AK, with a difference in denaturation temperature (T(m)) of 40 degrees C. Comparison of the crystal structures of TtAKbeta and the regulatory subunit of C. glutamicum AK showed that the well-packed hydrophobic core and high Pro content in loops contribute to the high thermostability of TtAKbeta.
Crystal structures of the regulatory subunit of Thr-sensitive aspartate kinase from Thermus thermophilus.,Yoshida A, Tomita T, Kono H, Fushinobu S, Kuzuyama T, Nishiyama M FEBS J. 2009 Jun;276(11):3124-36. Epub 2009 Apr 23. PMID:19490113<ref>PMID:19490113</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2dt9" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Flavobacterium thermophilum yoshida and oshima 1971]]
[[Category: Large Structures]]
[[Category: Aspartate kinase]]
[[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]]
[[Category: Transferase]]

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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