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| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8bgw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bgw OCA], [https://pdbe.org/8bgw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bgw RCSB], [https://www.ebi.ac.uk/pdbsum/8bgw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bgw ProSAT]</span></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=8bgw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bgw OCA], [https://pdbe.org/8bgw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bgw RCSB], [https://www.ebi.ac.uk/pdbsum/8bgw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bgw ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function ==
| |
| [https://www.uniprot.org/uniprot/A0A0D6H8R3_ALCXX A0A0D6H8R3_ALCXX]
| |
| <div style="background-color:#fffaf0;">
| |
| == Publication Abstract from PubMed ==
| |
| Quinol-dependent nitric oxide reductases (qNORs) are considered members of the respiratory heme-copper oxidase superfamily, are unique to bacteria, and are commonly found in pathogenic bacteria where they play a role in combating the host immune response. qNORs are also essential enzymes in the denitrification pathway, catalysing the reduction of nitric oxide to nitrous oxide. Here, we determine a 2.2 A cryoEM structure of qNOR from Alcaligenes xylosoxidans, an opportunistic pathogen and a denitrifying bacterium of importance in the nitrogen cycle. This high-resolution structure provides insight into electron, substrate, and proton pathways, and provides evidence that the quinol binding site not only contains the conserved His and Asp residues but also possesses a critical Arg (Arg720) observed in cytochrome bo(3), a respiratory quinol oxidase.
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| A 2.2 A cryoEM structure of a quinol-dependent NO Reductase shows close similarity to respiratory oxidases.,Flynn AJ, Antonyuk SV, Eady RR, Muench SP, Hasnain SS Nat Commun. 2023 Jun 9;14(1):3416. doi: 10.1038/s41467-023-39140-x. PMID:37296134<ref>PMID:37296134</ref>
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|
| |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
| |
| <div class="pdbe-citations 8bgw" style="background-color:#fffaf0;"></div>
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| == References ==
| |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
