View source for 28pn


==CryoEM structure of native quinol dependent Nitric Oxide Reductase at pH 8.0 on gold grid.==
<StructureSection load='28pn' size='340' side='right'caption='[[28pn]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[28pn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Achromobacter_xylosoxidans Achromobacter xylosoxidans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=28PN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=28PN FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=28pn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=28pn OCA], [https://pdbe.org/28pn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=28pn RCSB], [https://www.ebi.ac.uk/pdbsum/28pn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=28pn ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
The membrane-bound quinol-dependent nitric oxide reductases (qNORs), which are members of the respiratory heme-copper oxidase superfamily, are of major importance to food production, environment, and human health. They are unique to bacteria and catalyze N-N bond formation, converting nitric oxide (NO) to generate the enzymatic product, nitrous oxide (N(2)O), in agricultural and pathogenic conditions. High-resolution qNOR structures have been reported from two bacterial species, in which the molecular size of the protein was increased by the insertion of apocytochrome b(562) (BRIL) at the C-terminus to facilitate cryoEM structure determination. However, it remains uncertain how BRIL fusion alters the native structure of these metalloenzymes. Here, we present the first high-resolution structure of Achromobacter xylosoxidans qNOR (AxqNOR) determined without a fusion tag at two different pH values, revealing structural differences near the catalytic core as well as overall conformational changes between the native and fusion-tagged structures. The native enzyme shows a bell-shaped pH dependence of enzymatic activity, like nitrite reductase, the preceding enzyme in the denitrification pathway, which generates the substrate NO. In addition, we report structures of AxqNOR bound to quinol and hydroxyquinol that provide valuable insight into the potential electron transfer pathway originating from Trp718 to the redox centers.

CryoEM Structures of Native Quinol-Dependent Nitric Oxide Reductase in Resting and Quinol-Bound States.,Khaja FT, Mboukou A, Aspinall LP, Hawksworth CE, Eady RR, Antonyuk SV, Muench SP, Hasnain SS ACS Bio Med Chem Au. 2026 Mar 13;6(2):145-159. doi: , 10.1021/acsbiomedchemau.5c00245. eCollection 2026 Apr 15. PMID:42006251<ref>PMID:42006251</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 28pn" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Achromobacter xylosoxidans]]
[[Category: Large Structures]]
[[Category: Antonyuk SV]]
[[Category: Hasnain SS]]
[[Category: Khaja F]]
[[Category: Muench SP]]