9q3k
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of LarA-like nickel-pincer nucleotide cofactor-utilizing enzyme with a single catalytic histidine residue from Streptococcus plurextorum== | |
| + | <StructureSection load='9q3k' size='340' side='right'caption='[[9q3k]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9q3k]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus Streptococcus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9Q3K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9Q3K FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.2Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4EY:1-[(2R,3R,4S,5R)-3,4-BIS(OXIDANYL)-5-(PHOSPHONOOXYMETHYL)OXOLAN-2-YL]-5-METHANETHIOYL-PYRIDINE-3-CARBOTHIOIC+S-ACID'>4EY</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></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=9q3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9q3k OCA], [https://pdbe.org/9q3k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9q3k RCSB], [https://www.ebi.ac.uk/pdbsum/9q3k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9q3k ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The nickel pincer nucleotide (NPN) cofactor catalyzes the racemization/epimerization of alpha-hydroxy acids in enzymes of the LarA family. The established proton-coupled hydride transfer mechanism requires two catalytic histidine residues that alternately act as general acids and general bases. Notably, however, a fraction of LarA homologs (LarAHs) lack one of the active site histidine residues, replacing it with an asparaginyl side chain that cannot participate in acid/base catalysis. Here, we investigated two such LarAHs and solved their cryo-electron microscopic structures with and without loaded NPN cofactor, respectively. The structures revealed a consistent octameric assembly that is unprecedented in the LarA family and unveiled a new set of active site residues that likely recognize and process substrates differently from those of the well-studied LarAHs. Genomic context analysis suggested their potential involvement in carbohydrate metabolism. Together, these findings lay the groundwork for expanding the breadth of reactions and the range of mechanisms of LarA enzymes. | ||
| - | + | Structures of two LarA-like nickel-pincer nucleotide cofactor-utilizing enzymes with a single catalytic histidine residue.,Gatreddi S, Subramanian S, Sui D, Wang T, Urdiain-Arraiza J, Desguin B, Hausinger RP, Parent KN, Hu J bioRxiv [Preprint]. 2025 Aug 21:2025.08.19.671153. doi: , 10.1101/2025.08.19.671153. PMID:40894700<ref>PMID:40894700</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 9q3k" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Streptococcus]] | ||
| + | [[Category: Gatreddi S]] | ||
| + | [[Category: Hausinger RP]] | ||
| + | [[Category: Hu J]] | ||
| + | [[Category: Parent KN]] | ||
| + | [[Category: Subramanian S]] | ||
Current revision
Structure of LarA-like nickel-pincer nucleotide cofactor-utilizing enzyme with a single catalytic histidine residue from Streptococcus plurextorum
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