2zho

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[[Image:2zho.png|left|200px]]
 
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==Crystal structure of the regulatory subunit of aspartate kinase from Thermus thermophilus (ligand free form)==
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The line below this paragraph, containing "STRUCTURE_2zho", creates the "Structure Box" on the page.
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<StructureSection load='2zho' size='340' side='right'caption='[[2zho]], [[Resolution|resolution]] 2.98&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2zho]] is a 6 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=2ZHO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZHO FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.98&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2zho FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zho OCA], [https://pdbe.org/2zho PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zho RCSB], [https://www.ebi.ac.uk/pdbsum/2zho PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zho ProSAT]</span></td></tr>
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{{STRUCTURE_2zho| PDB=2zho | SCENE= }}
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zh/2zho_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2zho ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===Crystal structure of the regulatory subunit of aspartate kinase from Thermus thermophilus (ligand free form)===
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_19490113}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2zho" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 19490113 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19490113}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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[[2zho]] is a 6 chain structure with 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=2ZHO OCA].
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==Reference==
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<ref group="xtra">PMID:19490113</ref><ref group="xtra">PMID:16232547</ref><ref group="xtra">PMID:7773416</ref><references group="xtra"/>
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[[Category: Aspartate kinase]]
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[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
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[[Category: Kuzuyama, T.]]
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[[Category: Kuzuyama T]]
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[[Category: Nishiyama, M.]]
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[[Category: Nishiyama M]]
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[[Category: Tomita, T.]]
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[[Category: Tomita T]]
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[[Category: Yoshida, A.]]
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[[Category: Yoshida A]]
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[[Category: Act domain]]
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[[Category: Alternative initiation]]
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[[Category: Amino-acid biosynthesis]]
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[[Category: Diaminopimelate biosynthesis]]
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[[Category: Kinase]]
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[[Category: Lysine biosynthesis]]
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[[Category: Regulatory domain]]
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[[Category: Transferase]]
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Current revision

Crystal structure of the regulatory subunit of aspartate kinase from Thermus thermophilus (ligand free form)

PDB ID 2zho

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