4g09: Difference between revisions

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==The crystal structure of the C366S mutant of HDH from Brucella suis in complex with a substituted benzyl ketone==
==The crystal structure of the C366S mutant of HDH from Brucella suis in complex with a substituted benzyl ketone==
<StructureSection load='4g09' size='340' side='right' caption='[[4g09]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='4g09' size='340' side='right'caption='[[4g09]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4g09]] 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=4G09 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G09 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4g09]] 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=4G09 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G09 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0VD:(3S)-3-AMINO-1-[4-(BENZYLOXY)PHENYL]-4-(1H-IMIDAZOL-4-YL)BUTAN-2-ONE'>0VD</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.9&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4g07|4g07]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0VD:(3S)-3-AMINO-1-[4-(BENZYLOXY)PHENYL]-4-(1H-IMIDAZOL-4-YL)BUTAN-2-ONE'>0VD</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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">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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4g09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g09 OCA], [https://pdbe.org/4g09 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g09 RCSB], [https://www.ebi.ac.uk/pdbsum/4g09 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g09 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=4g09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g09 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4g09 RCSB], [http://www.ebi.ac.uk/pdbsum/4g09 PDBsum]</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;">
== 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<ref>PMID:24140957</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
== References ==
<references/>
__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-oxidoreductase inhibitor complex]]
[[Category: Rossmann fold]]
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