4ydr

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'''Unreleased structure'''
 
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The entry 4ydr is ON HOLD until Paper Publication
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==Crystal structure of oxidized homoserine dehydrogenase of Sulfolobus tokodaii==
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<StructureSection load='4ydr' size='340' side='right'caption='[[4ydr]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4ydr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfurisphaera_tokodaii_str._7 Sulfurisphaera tokodaii str. 7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YDR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YDR 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]] 1.6&#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=NA:SODIUM+ION'>NA</scene></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=4ydr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ydr OCA], [https://pdbe.org/4ydr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ydr RCSB], [https://www.ebi.ac.uk/pdbsum/4ydr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ydr ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DHOM_SULTO DHOM_SULTO] Catalyzes the conversion of L-aspartate-beta-semialdehyde (L-Asa) to L-homoserine (L-Hse), the third step in the biosynthesis of threonine and methionine from aspartate.<ref>PMID:29124164</ref> <ref>PMID:29636528</ref> <ref>PMID:35835834</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Homoserine dehydrogenase (HSD; 305 amino acid residues) catalyzes an NAD(P)-dependent reversible reaction between l-homoserine and aspartate 4-semialdehyde and is involved in the aspartate pathway. HSD from the hyperthermophilic archaeon Sulfolobus tokodaii was markedly activated (2.5-fold) by the addition of 0.8 mM dithiothreitol. The crystal structure of the homodimer indicated that the activation was caused by cleavage of the disulfide bond formed between two cysteine residues (C303) in the C-terminal regions of the two subunits.
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Authors: Goto, M., Yoshimune, K., Kaneko, R.
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Structural insight into activation of homoserine dehydrogenase from the archaeon Sulfolobus tokodaii via reduction.,Tomonaga Y, Kaneko R, Goto M, Ohshima T, Yoshimune K Biochem Biophys Rep. 2015 Jul 15;3:14-17. doi: 10.1016/j.bbrep.2015.07.006., eCollection 2015 Sep. PMID:29124164<ref>PMID:29124164</ref>
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Description: Crystal structure of oxidized homoserine dehydrogenase of Sulfolobus tokodaii
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Kaneko, R]]
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<div class="pdbe-citations 4ydr" style="background-color:#fffaf0;"></div>
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[[Category: Yoshimune, K]]
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== References ==
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[[Category: Goto, M]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Sulfurisphaera tokodaii str. 7]]
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[[Category: Goto M]]
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[[Category: Kaneko R]]
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[[Category: Yoshimune K]]

Current revision

Crystal structure of oxidized homoserine dehydrogenase of Sulfolobus tokodaii

PDB ID 4ydr

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