9q3j
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structures of LarA-like nickel-pincer nucleotide cofactor-utilizing enzyme with a single catalytic histidine residue from Blautia wexlerae== | |
| + | <StructureSection load='9q3j' size='340' side='right'caption='[[9q3j]], [[Resolution|resolution]] 3.15Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9q3j]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Blautia Blautia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9Q3J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9Q3J 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]] 3.15Å</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=9q3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9q3j OCA], [https://pdbe.org/9q3j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9q3j RCSB], [https://www.ebi.ac.uk/pdbsum/9q3j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9q3j ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A174QNZ5_9FIRM A0A174QNZ5_9FIRM] | ||
| + | <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 9q3j" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Blautia]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Gatreddi S]] | ||
| + | [[Category: Hausinger RP]] | ||
| + | [[Category: Hu J]] | ||
| + | [[Category: Parent KN]] | ||
| + | [[Category: Subramanian S]] | ||
Current revision
Structures of LarA-like nickel-pincer nucleotide cofactor-utilizing enzyme with a single catalytic histidine residue from Blautia wexlerae
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