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| | ==Crystal Structure of Medicago truncatula L-Histidinol Dehydrogenase in Complex with L-Histidinol== | | ==Crystal Structure of Medicago truncatula L-Histidinol Dehydrogenase in Complex with L-Histidinol== |
| - | <StructureSection load='5vlc' size='340' side='right' caption='[[5vlc]], [[Resolution|resolution]] 1.97Å' scene=''> | + | <StructureSection load='5vlc' size='340' side='right'caption='[[5vlc]], [[Resolution|resolution]] 1.97Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5vlc]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Barrel_medic Barrel medic]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VLC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VLC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5vlc]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Medicago_truncatula Medicago truncatula]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VLC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VLC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HSO:L-HISTIDINOL'>HSO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.97Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5vlb|5vlb]], [[5vld|5vld]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HSO:L-HISTIDINOL'>HSO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MTR_2g030520 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3880 Barrel medic])</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=5vlc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vlc OCA], [https://pdbe.org/5vlc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vlc RCSB], [https://www.ebi.ac.uk/pdbsum/5vlc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vlc 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/Histidinol_dehydrogenase Histidinol dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.23 1.1.1.23] </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=5vlc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vlc OCA], [http://pdbe.org/5vlc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vlc RCSB], [http://www.ebi.ac.uk/pdbsum/5vlc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vlc ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/G7IKX3_MEDTR G7IKX3_MEDTR]] Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.[PIRNR:PIRNR000099] | + | [https://www.uniprot.org/uniprot/G7IKX3_MEDTR G7IKX3_MEDTR] Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.[PIRNR:PIRNR000099] |
| | <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: Barrel medic]] | + | [[Category: Large Structures]] |
| - | [[Category: Histidinol dehydrogenase]] | + | [[Category: Medicago truncatula]] |
| - | [[Category: Dauter, Z]] | + | [[Category: Dauter Z]] |
| - | [[Category: Ruszkowski, M]] | + | [[Category: Ruszkowski M]] |
| - | [[Category: Histidine biosynthesis]]
| + | |
| - | [[Category: Nad binding protein]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Plant protein]]
| + | |
| - | [[Category: Zn2+ binding protein]]
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| Structural highlights
Function
G7IKX3_MEDTR Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.[PIRNR:PIRNR000099]
Publication Abstract from PubMed
Plants, lower eukaryotes, bacteria, and archaebacteria synthesise L-histidine (His) in a similar, multistep pathway that is absent in mammals. This makes the His biosynthetic route a promising target for herbicides, antifungal agents, and antibiotics. The last enzyme of the pathway, bifunctional L-histidinol dehydrogenase (HDH, EC 1.1.1.23), catalyses two oxidation reactions: from L-histidinol (HOL) to L-histidinaldehyde and from L-histidinaldehyde to His. Over the course of the reaction, HDH utilises two molecules of NAD+ as the hydride acceptor. The object of this study was the HDH enzyme from the model legume plant, Medicago truncatula (MtHDH). Three crystal structures complexed with imidazole, HOL, and His with NAD+ provided in-depth insights into the enzyme architecture, its active site, and the cofactor binding mode. The overall structure of MtHDH is similar to the two bacterial orthologues whose three-dimensional structures have been determined. The three snapshots, with the MtHDH enzyme captured in different states, visualise structural rearrangements that allow for NAD+ binding for the first time. Furthermore, the MtHDH complex with His and NAD+ displays the cofactor molecule situated in a way that would allow for a hydride transfer.
Structures of Medicago truncatula L-Histidinol Dehydrogenase Show Rearrangements Required for NAD+ Binding and the Cofactor Positioned to Accept a Hydride.,Ruszkowski M, Dauter Z Sci Rep. 2017 Sep 5;7(1):10476. doi: 10.1038/s41598-017-10859-0. PMID:28874718[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ruszkowski M, Dauter Z. Structures of Medicago truncatula L-Histidinol Dehydrogenase Show Rearrangements Required for NAD+ Binding and the Cofactor Positioned to Accept a Hydride. Sci Rep. 2017 Sep 5;7(1):10476. doi: 10.1038/s41598-017-10859-0. PMID:28874718 doi:http://dx.doi.org/10.1038/s41598-017-10859-0
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