6f4l: Difference between revisions
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<StructureSection load='6f4l' size='340' side='right' caption='[[6f4l]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='6f4l' size='340' side='right' caption='[[6f4l]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == 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> | <table><tr><td colspan='2'>[[6f4l]] 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=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> | </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='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='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='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> | <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> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Quinolinate synthase]] | [[Category: Quinolinate synthase]] | ||
[[Category: Thema]] | |||
[[Category: Fontecilla-Camps, J C]] | [[Category: Fontecilla-Camps, J C]] | ||
[[Category: Volbeda, A]] | [[Category: Volbeda, A]] | ||
Latest revision as of 08:56, 30 May 2018
Structure of quinolinate synthase with inhibitor-derived quinolinateStructure of quinolinate synthase with inhibitor-derived quinolinate
Structural highlights
Function[NADA_THEMA] Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate (By similarity). Publication Abstract from PubMedNadA 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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