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| | <StructureSection load='4ydr' size='340' side='right'caption='[[4ydr]], [[Resolution|resolution]] 1.60Å' scene=''> | | <StructureSection load='4ydr' size='340' side='right'caption='[[4ydr]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ydr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Sulto Sulto]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YDR FirstGlance]. <br> | + | <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> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 1.6Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hom, STK_15190 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273063 SULTO])</td></tr>
| + | <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> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Homoserine_dehydrogenase Homoserine dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.3 1.1.1.3] </span></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=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> |
| - | <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=4ydr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ydr OCA], [http://pdbe.org/4ydr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ydr RCSB], [http://www.ebi.ac.uk/pdbsum/4ydr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ydr ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Homoserine dehydrogenase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Sulto]] | + | [[Category: Sulfurisphaera tokodaii str. 7]] |
| - | [[Category: Goto, M]] | + | [[Category: Goto M]] |
| - | [[Category: Kaneko, R]] | + | [[Category: Kaneko R]] |
| - | [[Category: Yoshimune, K]] | + | [[Category: Yoshimune K]] |
| - | [[Category: Oxidized form]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
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.[1] [2] [3]
Publication Abstract from PubMed
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.
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[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tomonaga Y, Kaneko R, Goto M, Ohshima T, Yoshimune K. Structural insight into activation of homoserine dehydrogenase from the archaeon Sulfolobus tokodaii via reduction. Biochem Biophys Rep. 2015 Jul 15;3:14-17. doi: 10.1016/j.bbrep.2015.07.006., eCollection 2015 Sep. PMID:29124164 doi:http://dx.doi.org/10.1016/j.bbrep.2015.07.006
- ↑ Ogata K, Yajima Y, Nakamura S, Kaneko R, Goto M, Ohshima T, Yoshimune K. Inhibition of homoserine dehydrogenase by formation of a cysteine-NAD covalent complex. Sci Rep. 2018 Apr 10;8(1):5749. doi: 10.1038/s41598-018-24063-1. PMID:29636528 doi:http://dx.doi.org/10.1038/s41598-018-24063-1
- ↑ Kubota T, Kurihara E, Watanabe K, Ogata K, Kaneko R, Goto M, Ohshima T, Yoshimune K. Conformational changes in the catalytic region are responsible for heat-induced activation of hyperthermophilic homoserine dehydrogenase. Commun Biol. 2022 Jul 14;5(1):704. doi: 10.1038/s42003-022-03656-7. PMID:35835834 doi:http://dx.doi.org/10.1038/s42003-022-03656-7
- ↑ Tomonaga Y, Kaneko R, Goto M, Ohshima T, Yoshimune K. Structural insight into activation of homoserine dehydrogenase from the archaeon Sulfolobus tokodaii via reduction. Biochem Biophys Rep. 2015 Jul 15;3:14-17. doi: 10.1016/j.bbrep.2015.07.006., eCollection 2015 Sep. PMID:29124164 doi:http://dx.doi.org/10.1016/j.bbrep.2015.07.006
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