View source for 9pfw


==Crystal structure of selenomethionine-substituted N-oxygenase RohS from Pseudomonas syringae pv. tomato str. DC3000 (PstoRohS)==
<StructureSection load='9pfw' size='340' side='right'caption='[[9pfw]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9pfw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_syringae_pv._tomato_str._DC3000 Pseudomonas syringae pv. tomato str. DC3000]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9PFW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9PFW 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]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=9pfw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9pfw OCA], [https://pdbe.org/9pfw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9pfw RCSB], [https://www.ebi.ac.uk/pdbsum/9pfw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9pfw ProSAT]</span></td></tr>
</table>
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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 9pfw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas syringae pv. tomato str. DC3000]]
[[Category: Higgins MA]]
[[Category: Ryan KS]]
[[Category: Wei Z-W]]