View source for 9bq0


==Complex structure of protein crystal of Tri17 with ATP==
<StructureSection load='9bq0' size='340' side='right'caption='[[9bq0]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9bq0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_tsukubensis Streptomyces tsukubensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9BQ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9BQ0 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]] 2.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=9bq0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9bq0 OCA], [https://pdbe.org/9bq0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9bq0 RCSB], [https://www.ebi.ac.uk/pdbsum/9bq0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9bq0 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Azides are energy-rich compounds with diverse representation in a broad range of scientific disciplines, including material science, synthetic chemistry, pharmaceutical science and chemical biology. Despite ubiquitous usage of the azido group, the underlying biosynthetic pathways for its formation remain largely unknown. Here we report the characterization of an enzymatic route for de novo azide construction. We demonstrate that Tri17, a promiscuous ATP- and nitrite-dependent enzyme, catalyses organic azide synthesis through sequential N-nitrosation and dehydration of aryl hydrazines. Through biochemical, structural and computational analyses, we further propose a plausible molecular mechanism for azide synthesis that sets the stage for future biocatalytic applications and biosynthetic pathway engineering.

Enzymatic synthesis of azide by a promiscuous N-nitrosylase.,Del Rio Flores A, Zhai R, Kastner DW, Seshadri K, Yang S, De Matias K, Shen Y, Cai W, Narayanamoorthy M, Do NB, Xue Z, Marzooqi DA, Kulik HJ, Zhang W Nat Chem. 2024 Sep 27. doi: 10.1038/s41557-024-01646-2. PMID:39333393<ref>PMID:39333393</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9bq0" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces tsukubensis]]
[[Category: Zhai R]]
[[Category: Zhang W]]