5avo
From Proteopedia
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==Crystal structure of the reduced form of homoserine dehydrogenase from Sulfolobus tokodaii.== | ==Crystal structure of the reduced form of homoserine dehydrogenase from Sulfolobus tokodaii.== | ||
| - | <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 [ | + | <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=' | + | </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='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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</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;"> | ||
| + | == 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<ref>PMID:29124164</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5avo" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Sulfurisphaera tokodaii str. 7]] |
| - | [[Category: Goto | + | [[Category: Goto M]] |
| - | [[Category: Kaneko | + | [[Category: Kaneko R]] |
| - | [[Category: Yoshimune | + | [[Category: Yoshimune K]] |
| - | + | ||
| - | + | ||
Current revision
Crystal structure of the reduced form of homoserine dehydrogenase from Sulfolobus tokodaii.
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