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Structure paper

TitleStructure of the - respiratory supercomplex from .
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 120, Issue 40, Page e2307093120, Year 2023
Publish dateOct 3, 2023
AuthorsJustin M Di Trani / Andreea A Gheorghita / Madison Turner / Peter Brzezinski / Pia Ädelroth / Siavash Vahidi / P Lynne Howell / John L Rubinstein /
PubMed AbstractEnergy 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 ...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.
External linksProc Natl Acad Sci U S A / PubMed:37751552 / PubMed Central
MethodsEM (single particle)
Resolution2.3 - 3.0 Å
Structure data

40601

8smr

EMDB-40601, PDB-8smr:
cytochrome bc1-cbb3 supercomplex from Pseudomonas aeruginosa
Method: EM (single particle) / Resolution: 2.7 Å

40625

8snh

EMDB-40625, PDB-8snh:
cytochrome bc1-cbb3 supercomplex from Pseudomonas aeruginosa
Method: EM (single particle) / Resolution: 2.7 Å

EMDB-40626: cytochrome bc1 complex from Pseudomonas aeruginosa
Method: EM (single particle) / Resolution: 2.3 Å

EMDB-40627: cytochrome bc1-cbb3 supercomplex from Pseudomonas aeruginosa (Locally refined cytochrome cbb3)
Method: EM (single particle) / Resolution: 2.8 Å

EMDB-40637: cytochrome bc1 complex from Pseudomonas aeruginosa (Locally refined bc1 monomer with Rieske head domain in b state)
Method: EM (single particle) / Resolution: 2.3 Å

EMDB-40638: cytochrome bc1 complex from Pseudomonas aeruginosa (Locally refined bc1 monomer with Rieske head domain in c state)
Method: EM (single particle) / Resolution: 2.4 Å

EMDB-40643: cytochrome bc1-cbb3 supercomplex from Pseudomonas aeruginosa (Locally refined cytochrome cbb3 with CcoP1 isoform)
Method: EM (single particle) / Resolution: 3.0 Å

EMDB-40645: cytochrome bc1-cbb3 supercomplex from Pseudomonas aeruginosa (Locally refined cytochrome cbb3 with CcoP2 isoform)
Method: EM (single particle) / Resolution: 3.0 Å

Chemicals

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER / Iron–sulfur cluster

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE / Heme B

ChemComp-U10:
UBIQUINONE-10 / Coenzyme Q10

ChemComp-I7Y:
(2R)-2-(methoxymethyl)-4-{[(25R)-spirost-5-en-3beta-yl]oxy}butyl 4-O-alpha-D-glucopyranosyl-beta-D-glucopyranoside

ChemComp-HEC:
HEME C / Heme C

ChemComp-CU:
COPPER (II) ION / Copper

ChemComp-CA:
Unknown entry

Source
  • pseudomonas aeruginosa (bacteria)
KeywordsMEMBRANE PROTEIN / Electron transport chain / Supercomplex / Pseudomonas aeruginosa

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