9or1: Difference between revisions

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New page: '''Unreleased structure''' The entry 9or1 is ON HOLD Authors: Description: Category: Unreleased Structures
 
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'''Unreleased structure'''


The entry 9or1 is ON HOLD
==N-hydroxylamine dehydratase (NohD) H2F/F4P/P5S/R6Y/A59N/R144Y/V96A/D172E/L172Q/D173P/R176V (P1/P2/A1/A2/A3) mutant crystal structure with heme and N-hydroxylated ornithine==
<StructureSection load='9or1' size='340' side='right'caption='[[9or1]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9or1]] 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=9OR1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9OR1 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=ONH:N~5~-HYDROXY-L-ORNITHINE'>ONH</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=9or1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9or1 OCA], [https://pdbe.org/9or1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9or1 RCSB], [https://www.ebi.ac.uk/pdbsum/9or1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9or1 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


Authors:  
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>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 9or1" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Actinomadura]]
[[Category: Large Structures]]
[[Category: Du YL]]
[[Category: Higgins MA]]
[[Category: Hoffarth ER]]
[[Category: Ryan KS]]
[[Category: Shi X]]
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