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6f4l
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of quinolinate synthase with inhibitor-derived quinolinate== | |
| + | <StructureSection load='6f4l' size='340' side='right' caption='[[6f4l]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6f4l]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F4L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6F4L FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</scene>, <scene name='pdbligand=NTM:QUINOLINIC+ACID'>NTM</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></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=6f4l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f4l OCA], [http://pdbe.org/6f4l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f4l RCSB], [http://www.ebi.ac.uk/pdbsum/6f4l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f4l ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://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;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | NadA is a multifunctional enzyme that condenses dihydroxyacetone phosphate (DHAP) with iminoaspartate (IA) to generate quinolinic acid (QA), the universal precursor of the nicotinamide adenine dinucleotide (NAD(P)) cofactor. Using X-ray crystallography, we have (i) characterized two of the reaction intermediates of QA synthesis using a "pH-shift" approach and a slowly reacting Thermotoga maritima NadA variant and (ii) observed the QA product, resulting from the degradation of an intermediate analogue, bound close to the entrance of a long tunnel leading to the solvent medium. We have also used molecular docking to propose a condensation mechanism between DHAP and IA based on two previously published Pyrococcus horikoshi NadA structures. The combination of reported data and our new results provide a structure-based complete catalytic sequence of QA synthesis by NadA. | ||
| - | + | Crystallographic Trapping of Reaction Intermediates in Quinolinic Acid Synthesis by NadA.,Volbeda A, Saez Cabodevilla J, Darnault C, Gigarel O, Han TH, Renoux O, Hamelin O, Ollagnier-de-Choudens S, Amara P, Fontecilla-Camps JC ACS Chem Biol. 2018 Apr 19. doi: 10.1021/acschembio.7b01104. PMID:29641168<ref>PMID:29641168</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6f4l" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Quinolinate synthase]] | ||
| + | [[Category: Fontecilla-Camps, J C]] | ||
[[Category: Volbeda, A]] | [[Category: Volbeda, A]] | ||
| - | [[Category: | + | [[Category: Iron sulfur cluster]] |
| + | [[Category: Nad biosynthesis]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 05:37, 25 April 2018
Structure of quinolinate synthase with inhibitor-derived quinolinate
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