8SNH
cytochrome bc1-cbb3 supercomplex from Pseudomonas aeruginosa
Summary for 8SNH
| Entry DOI | 10.2210/pdb8snh/pdb |
| EMDB information | 40625 |
| Descriptor | cytochrome-c oxidase, CALCIUM ION, PROTOPORPHYRIN IX CONTAINING FE, ... (15 entities in total) |
| Functional Keywords | electron transport chain, supercomplex, pseudomonas aeruginosa, membrane protein |
| Biological source | Pseudomonas aeruginosa More |
| Total number of polymer chains | 13 |
| Total formula weight | 371910.80 |
| Authors | Di Trani, J.M.,Rubinstein, J.L. (deposition date: 2023-04-27, release date: 2023-10-11, Last modification date: 2025-05-14) |
| Primary citation | Di Trani, J.M.,Gheorghita, A.A.,Turner, M.,Brzezinski, P.,Adelroth, P.,Vahidi, S.,Howell, P.L.,Rubinstein, J.L. Structure of the bc 1 - cbb 3 respiratory supercomplex from Pseudomonas aeruginosa. Proc.Natl.Acad.Sci.USA, 120:e2307093120-e2307093120, 2023 Cited by PubMed Abstract: Energy 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 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 SC that forms between the quinol:cytochrome oxidoreductase (cytochrome ) and one of the organism's terminal oxidases, cytochrome , which is found only in some bacteria. Remarkably, the SC structure also includes two intermediate electron carriers: a diheme cytochrome and a single heme cytochrome . Together, these proteins allow electron transfer from ubiquinol in cytochrome to oxygen in cytochrome . We also present evidence that different isoforms of cytochrome 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 - SCs also exist in other bacterial pathogens. PubMed: 37751552DOI: 10.1073/pnas.2307093120 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.7 Å) |
Structure validation
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