9pfx: Difference between revisions
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==Crystal structure of native HDO-family N-oxygenase RohS from Pseudomonas brassicacearum strain DF41 (PbrRohS)== | |||
<StructureSection load='9pfx' size='340' side='right'caption='[[9pfx]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9pfx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_brassicacearum Pseudomonas brassicacearum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9PFX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9PFX 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]] 2.2Å</td></tr> | |||
<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></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=9pfx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9pfx OCA], [https://pdbe.org/9pfx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9pfx RCSB], [https://www.ebi.ac.uk/pdbsum/9pfx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9pfx ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The nitro group is an important functional group found in the nitroimidazoles, antibiotic therapeutics for anaerobic pathogens. In the biosynthetic pathway to the nitroimidazole antibiotic azomycin, a nitro-forming enzyme RohS - a member of the heme-oxygenase-like dimetal/domain-containing oxidase/oxygenase (HDO) family - catalyzes a six-electron oxidation of 2-aminoimidazole to 2-nitroimidazole. Here we present the 2.20 A resolution crystal structure of RohS and identify a potential active site pocket consisting of seven key residues important for metal coordination. By comparing the structures and sequences of two RohS homologs - one functionally active and one inactive - we convert the inactive RohS to its active form, thus revealing a key residue for metal coordination in RohS catalysis. Altogether, our work provides structural basis for further mechanistic investigation of this six-electron oxidation process and provides insight into the expanding repertoire of the HDO protein family and nitro-formation N-oxygenases. | |||
Crystal structure of RohS, a heme-oxygenase-like N-oxygenase from azomycin biosynthesis.,Wei ZW, Salamon P, Higgins MA, Ryan KS J Biol Chem. 2026 Mar 20:111389. doi: 10.1016/j.jbc.2026.111389. PMID:41866038<ref>PMID:41866038</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 9pfx" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pseudomonas brassicacearum]] | |||
[[Category: Higgins MA]] | |||
[[Category: Ryan KS]] | |||
[[Category: Wei Z-W]] | |||
Latest revision as of 15:54, 1 April 2026
Crystal structure of native HDO-family N-oxygenase RohS from Pseudomonas brassicacearum strain DF41 (PbrRohS)
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