5ktm
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Pyrococcus horikoshii quinolinate synthase (NadA) with a bound Fe4S4 cluster== | |
| + | <StructureSection load='5ktm' size='340' side='right' caption='[[5ktm]], [[Resolution|resolution]] 1.44Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5ktm]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KTM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KTM 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=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5kts|5kts]], [[5ktt|5ktt]], [[5ktr|5ktr]], [[5kto|5kto]], [[5ktn|5ktn]], [[5ktp|5ktp]]</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=5ktm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ktm OCA], [http://pdbe.org/5ktm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ktm RCSB], [http://www.ebi.ac.uk/pdbsum/5ktm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ktm ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/NADA_PYRHO NADA_PYRHO]] Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate (By similarity). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The quinolinate synthase of prokaryotes and photosynthetic eukaryotes, NadA, contains a [4Fe-4S] cluster with unknown function. We report crystal structures of Pyrococcus horikoshii NadA in complex with dihydroxyacetone phosphate (DHAP), iminoaspartate analogues, and quinolinate. DHAP adopts a nearly planar conformation and chelates the [4Fe-4S] cluster via its keto and hydroxyl groups. The active site architecture suggests that the cluster acts as a Lewis acid in enediolate formation, like zinc in class II aldolases. The DHAP and putative iminoaspartate structures suggest a model for a condensed intermediate. The ensemble of structures suggests a two-state system, which may be exploited in early steps. | ||
| - | + | Crystal Structures of the Iron-Sulfur Cluster-Dependent Quinolinate Synthase in Complex with Dihydroxyacetone Phosphate, Iminoaspartate Analogues, and Quinolinate.,Fenwick MK, Ealick SE Biochemistry. 2016 Jul 22. PMID:27404889<ref>PMID:27404889</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5ktm" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Quinolinate synthase]] | ||
| + | [[Category: Ealick, S E]] | ||
| + | [[Category: Fenwick, M K]] | ||
| + | [[Category: Biosynthetic enzyme]] | ||
| + | [[Category: Dehydratase]] | ||
| + | [[Category: Holoenzyme]] | ||
| + | [[Category: Iron-sulfur cluster]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 15:48, 27 July 2016
Crystal structure of Pyrococcus horikoshii quinolinate synthase (NadA) with a bound Fe4S4 cluster
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