6f48: Difference between revisions
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==Structure of quinolinate synthase with reaction intermediates X and Y== | |||
<StructureSection load='6f48' size='340' side='right' caption='[[6f48]], [[Resolution|resolution]] 1.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6f48]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F48 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6F48 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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=XQB:2-imino,3-carboxy,5-hydroxy,6-oxo+hexanoic+acid'>XQB</scene>, <scene name='pdbligand=YQA:5-hydroxy,-4,5-dihydroquinolinate'>YQA</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=2336 ATCC 43589])</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=6f48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f48 OCA], [http://pdbe.org/6f48 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f48 RCSB], [http://www.ebi.ac.uk/pdbsum/6f48 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f48 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 6f48" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Atcc 43589]] | |||
[[Category: Quinolinate synthase]] | |||
[[Category: Fontecilla-Camps, J C]] | |||
[[Category: Volbeda, A]] | [[Category: Volbeda, A]] | ||
[[Category: | [[Category: Iron sulfur cluster]] | ||
[[Category: Nad biosynthesis]] | |||
[[Category: Transferase]] | |||
Latest revision as of 08:55, 30 May 2018
Structure of quinolinate synthase with reaction intermediates X and YStructure of quinolinate synthase with reaction intermediates X and Y
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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