9oqs

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Current revision (19:26, 4 December 2025) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 9oqs is ON HOLD until Paper Publication
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==N-hydroxylamine dehydratase (NohD) crystal structure with heme==
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<StructureSection load='9oqs' size='340' side='right'caption='[[9oqs]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[9oqs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinomadura Actinomadura]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9OQS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9OQS FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9oqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9oqs OCA], [https://pdbe.org/9oqs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9oqs RCSB], [https://www.ebi.ac.uk/pdbsum/9oqs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9oqs ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Enzymes that form nitrogen-nitrogen bonds are employed in natural product biosynthesis and the nitrogen cycle. Piperazate synthase forms the cyclic hydrazine l-piperazic acid from l-N(5)-OH-ornithine, using heme as a cofactor. In this work, we discover sequence-related enzyme NohD that instead reacts with l-N(5)-OH-ornithine to release ammonia, and we solve its structure to 1.4 A resolution. We then employ structure-guided site-directed mutagenesis to endow variants of NohD with piperazate synthase activity. Crystal structures of the NohD variants reveal how the heme propionate changes conformation, positioning it upward toward the amino nitrogen, where it is likely to activate the amine for N-N bond-formation. This study highlights a key structural requirement for N-N bond-formation and sets the stage for the development of new N-N-bond-forming catalysts.
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Authors:
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Conversion of a Heme-Dependent Dehydratase to a Piperazate Synthase Reveals the Role of the Heme Propionate Group in N-N Bond-Formation.,Higgins MA, Mirotadze N, Shi X, Hoffarth ER, Du YL, Ryan KS J Am Chem Soc. 2025 Oct 29;147(43):39160-39168. doi: 10.1021/jacs.5c08886. Epub , 2025 Oct 16. PMID:41101755<ref>PMID:41101755</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 9oqs" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Actinomadura]]
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[[Category: Large Structures]]
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[[Category: Du YL]]
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[[Category: Higgins MA]]
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[[Category: Hoffarth ER]]
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[[Category: Ryan KS]]
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[[Category: Shi X]]

Current revision

N-hydroxylamine dehydratase (NohD) crystal structure with heme

PDB ID 9oqs

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