4g07

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==The crystal structure of the C366S mutant of HDH from Brucella suis==
==The crystal structure of the C366S mutant of HDH from Brucella suis==
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<StructureSection load='4g07' size='340' side='right' caption='[[4g07]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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<StructureSection load='4g07' size='340' side='right'caption='[[4g07]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<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>
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<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>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4g09|4g09]]</td></tr>
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<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>
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<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>
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<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>
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<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>
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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=4g07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g07 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4g07 RCSB], [http://www.ebi.ac.uk/pdbsum/4g07 PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[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).
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[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).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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<ref>PMID:24140957</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Brusu]]
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[[Category: Brucella suis 1330]]
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[[Category: Histidinol dehydrogenase]]
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[[Category: Large Structures]]
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[[Category: Ambrosio, K D]]
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[[Category: D'Ambrosio K]]
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[[Category: Simone, G De]]
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[[Category: De Simone G]]
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[[Category: L-histidinol dehydrogenase]]
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[[Category: Oxidoreductase]]
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[[Category: Rossmann fold]]
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Current revision

The crystal structure of the C366S mutant of HDH from Brucella suis

PDB ID 4g07

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