8smr
cytochrome bc1-cbb3 supercomplex from Pseudomonas aeruginosacytochrome bc1-cbb3 supercomplex from Pseudomonas aeruginosa
Structural highlights
FunctionA0A069Q0N5_PSEAI Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.[ARBA:ARBA00002444] Publication Abstract from PubMedEnergy conversion by electron transport chains occurs through the sequential transfer of electrons between protein complexes and intermediate electron carriers, creating the proton motive force that enables ATP synthesis and membrane transport. These protein complexes can also form higher order assemblies known as respiratory supercomplexes (SCs). The electron transport chain of the opportunistic pathogen Pseudomonas aeruginosa is closely linked with its ability to invade host tissue, tolerate harsh conditions, and resist antibiotics but is poorly characterized. Here, we determine the structure of a P. aeruginosa SC that forms between the quinol:cytochrome c oxidoreductase (cytochrome bc(1)) and one of the organism's terminal oxidases, cytochrome cbb(3), which is found only in some bacteria. Remarkably, the SC structure also includes two intermediate electron carriers: a diheme cytochrome c(4) and a single heme cytochrome c(5). Together, these proteins allow electron transfer from ubiquinol in cytochrome bc(1) to oxygen in cytochrome cbb(3). We also present evidence that different isoforms of cytochrome cbb(3) can participate in formation of this SC without changing the overall SC architecture. Incorporating these different subunit isoforms into the SC would allow the bacterium to adapt to different environmental conditions. Bioinformatic analysis focusing on structural motifs in the SC suggests that cytochrome bc(1)-cbb(3) SCs also exist in other bacterial pathogens. Structure of the bc(1)-cbb(3) respiratory supercomplex from Pseudomonas aeruginosa.,Di Trani JM, Gheorghita AA, Turner M, Brzezinski P, Adelroth P, Vahidi S, Howell PL, Rubinstein JL Proc Natl Acad Sci U S A. 2023 Oct 3;120(40):e2307093120. doi: , 10.1073/pnas.2307093120. Epub 2023 Sep 26. PMID:37751552[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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