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| | <StructureSection load='5avo' size='340' side='right'caption='[[5avo]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='5avo' size='340' side='right'caption='[[5avo]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5avo]] 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=5AVO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AVO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5avo]] 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=5AVO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AVO FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ydr|4ydr]]</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]] 1.8Å</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5avo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5avo OCA], [https://pdbe.org/5avo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5avo RCSB], [https://www.ebi.ac.uk/pdbsum/5avo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5avo 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/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>
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| - | <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=5avo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5avo OCA], [http://pdbe.org/5avo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5avo RCSB], [http://www.ebi.ac.uk/pdbsum/5avo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5avo 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: Oxidoreductase]]
| + | |
| - | [[Category: Reduced form]]
| + | |
| 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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