|
|
| Line 1: |
Line 1: |
| | | | |
| | ==The crystal structure of the C366S mutant of HDH from Brucella suis== | | ==The crystal structure of the C366S mutant of HDH from Brucella suis== |
| - | <StructureSection load='4g07' size='340' side='right' caption='[[4g07]], [[Resolution|resolution]] 1.95Å' scene=''> | + | <StructureSection load='4g07' size='340' side='right'caption='[[4g07]], [[Resolution|resolution]] 1.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4g07]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Brusu Brusu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G07 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G07 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4g07]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Brucella_suis_1330 Brucella suis 1330]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G07 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G07 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4g09|4g09]]</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=4g07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g07 OCA], [https://pdbe.org/4g07 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g07 RCSB], [https://www.ebi.ac.uk/pdbsum/4g07 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g07 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hisD, BR0252, BS1330_I0253 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=204722 BRUSU])</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=4g07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g07 OCA], [http://pdbe.org/4g07 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4g07 RCSB], [http://www.ebi.ac.uk/pdbsum/4g07 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4g07 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HISX_BRUSU HISX_BRUSU]] Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine (By similarity). | + | [https://www.uniprot.org/uniprot/HISX_BRUSU HISX_BRUSU] Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 25: |
Line 22: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Brusu]] | + | [[Category: Brucella suis 1330]] |
| - | [[Category: Histidinol dehydrogenase]] | + | [[Category: Large Structures]] |
| - | [[Category: Ambrosio, K D]] | + | [[Category: D'Ambrosio K]] |
| - | [[Category: Simone, G De]] | + | [[Category: De Simone G]] |
| - | [[Category: L-histidinol dehydrogenase]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Rossmann fold]]
| + | |
| Structural highlights
Function
HISX_BRUSU Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine (By similarity).
Publication Abstract from PubMed
l-histidinol dehydrogenase from Brucella suis (BsHDH) is an enzyme involved in the histidine biosynthesis pathway which is absent in mammals, thus representing a very interesting target for the development of anti-Brucella agents. In this paper we report the crystallographic structure of a mutated form of BsHDH both in its unbound form and in complex with a nanomolar inhibitor. These studies provide the first structural background for the rational design of potent HDH inhibitors, thus offering new hints for clinical applications.
Structural basis for the rational design of new anti-Brucella agents: The crystal structure of the C366S mutant of l-histidinol dehydrogenase from Brucella suis.,D'ambrosio K, Lopez M, Dathan NA, Ouahrani-Bettache S, Kohler S, Ascione G, Monti SM, Winum JY, De Simone G Biochimie. 2013 Oct 17. pii: S0300-9084(13)00349-0. doi:, 10.1016/j.biochi.2013.09.028. PMID:24140957[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ D'ambrosio K, Lopez M, Dathan NA, Ouahrani-Bettache S, Kohler S, Ascione G, Monti SM, Winum JY, De Simone G. Structural basis for the rational design of new anti-Brucella agents: The crystal structure of the C366S mutant of l-histidinol dehydrogenase from Brucella suis. Biochimie. 2013 Oct 17. pii: S0300-9084(13)00349-0. doi:, 10.1016/j.biochi.2013.09.028. PMID:24140957 doi:http://dx.doi.org/10.1016/j.biochi.2013.09.028
|
