View source for 9ufw


==Ubiquinol Binding Site of Cytochrome bo3 from Acinetobacter baumannii==
<StructureSection load='9ufw' size='340' side='right'caption='[[9ufw]], [[Resolution|resolution]] 3.12&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9ufw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baumannii Acinetobacter baumannii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9UFW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9UFW 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]] 3.12&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PE:1,2-DIACYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE'>3PE</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=HEO:HEME+O'>HEO</scene>, <scene name='pdbligand=LMG:1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE'>LMG</scene>, <scene name='pdbligand=UQ8:UBIQUINONE-8'>UQ8</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=9ufw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9ufw OCA], [https://pdbe.org/9ufw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9ufw RCSB], [https://www.ebi.ac.uk/pdbsum/9ufw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9ufw ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Heme-copper oxidases (heme-copper oxidoreductases) are terminal oxidases that couple oxygen reduction to proton pumping for ATP synthesis. Although our previous work has elucidated the structure and proton transfer mechanism of the Escherichia coli cytochrome bo(3) ubiquinol oxidase, the quinone dynamics and structural diversity across heme-copper oxidoreductases remain unclear. Here, we report the high-resolution cryo-EM structures of cytochrome bo(3) ubiquinol oxidase from the pathogen Acinetobacter baumannii. We captured four distinct conformational states of its native ubiquinone-8 substrate within the binding pocket. Comparative analysis revealed that conformational transitions of the substrate are directly coupled to movements of the transmembrane 0 helix. Notably, in the locked state, the substrate headgroup is stabilized by specific hydrogen bonds and adopts a distinct depth and orientation. In addition, a unique hairpin-like loop was identified in subunit II, a specific feature absent in the homologs. Our observations not only provide structural details of a pathogenic respiratory terminal oxidase but also reveal a dynamic substrate catalytic mechanism, highlighting potential avenues for targeting bacterial energy metabolism.

Structure of Acinetobacter baumannii cytochrome bo(3) ubiquinol oxidase.,Li Q, Hao R, Zhu J, Li J J Biol Chem. 2026 Apr;302(4):111324. doi: 10.1016/j.jbc.2026.111324. Epub 2026 , Feb 26. PMID:41759743<ref>PMID:41759743</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9ufw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Acinetobacter baumannii]]
[[Category: Large Structures]]
[[Category: Li J]]
[[Category: Zhu JP]]