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| | <StructureSection load='6i0r' size='340' side='right'caption='[[6i0r]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='6i0r' size='340' side='right'caption='[[6i0r]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6i0r]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thema Thema]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6I0R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6I0R FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6i0r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6I0R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6I0R FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=H2S:HYDROSULFURIC+ACID'>H2S</scene>, <scene name='pdbligand=QAT:5-mercaptopyridine-2,3-dicarboxylic+acid'>QAT</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]] 2.1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6i0k|6i0k]], [[6i0p|6i0p]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=H2S:HYDROSULFURIC+ACID'>H2S</scene>, <scene name='pdbligand=QAT:5-mercaptopyridine-2,3-dicarboxylic+acid'>QAT</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nadA, TM_1644 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 THEMA])</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=6i0r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6i0r OCA], [https://pdbe.org/6i0r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6i0r RCSB], [https://www.ebi.ac.uk/pdbsum/6i0r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6i0r 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/Quinolinate_synthase Quinolinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.72 2.5.1.72] </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=6i0r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6i0r OCA], [http://pdbe.org/6i0r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6i0r RCSB], [http://www.ebi.ac.uk/pdbsum/6i0r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6i0r ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/NADA_THEMA NADA_THEMA]] Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate (By similarity). | + | [https://www.uniprot.org/uniprot/NADA_THEMA NADA_THEMA] Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Quinolinate synthase]] | + | [[Category: Thermotoga maritima MSB8]] |
| - | [[Category: Thema]]
| + | [[Category: Fontecilla-Camps JC]] |
| - | [[Category: Fontecilla-Camps, J C]] | + | [[Category: Volbeda A]] |
| - | [[Category: Volbeda, A]] | + | |
| - | [[Category: Iron sulfur cluster]]
| + | |
| - | [[Category: Nad biosynthesis]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
NADA_THEMA Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate (By similarity).
Publication Abstract from PubMed
Quinolinate synthase (NadA) is a [4Fe-4S] cluster-containing enzyme involved in the formation of quinolinic acid, the precursor of the essential NAD coenzyme. Here, we report the synthesis and activity of derivatives of the first inhibitor of NadA. Using multidisciplinary approaches we have investigated their action mechanism and discovered additional specific inhibitors of this enzyme.
Design of specific inhibitors of quinolinate synthase based on [4Fe-4S] cluster coordination.,Saez Cabodevilla J, Volbeda A, Hamelin O, Latour JM, Gigarel O, Clemancey M, Darnault C, Reichmann D, Amara P, Fontecilla-Camps JC, Ollagnier de Choudens S Chem Commun (Camb). 2019 Mar 11. doi: 10.1039/c8cc09023h. PMID:30855610[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Saez Cabodevilla J, Volbeda A, Hamelin O, Latour JM, Gigarel O, Clemancey M, Darnault C, Reichmann D, Amara P, Fontecilla-Camps JC, Ollagnier de Choudens S. Design of specific inhibitors of quinolinate synthase based on [4Fe-4S] cluster coordination. Chem Commun (Camb). 2019 Mar 11. doi: 10.1039/c8cc09023h. PMID:30855610 doi:http://dx.doi.org/10.1039/c8cc09023h
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