Insights into conformational changes in cytochrome b during the early steps of its maturation

Author:

Carlström Andreas12ORCID,Ott Martin12ORCID

Affiliation:

1. Department of Biochemistry and Biophysics Stockholm University Sweden

2. Department of Medical Biochemistry and Cell Biology, Institute of Biomedicine University of Gothenburg Sweden

Abstract

Membrane proteins carrying redox cofactors are key subunits of respiratory chain complexes, yet the exact path of their folding and maturation remains poorly understood. Here, using cryo‐EM and structure prediction via Alphafold2, we generated models of early assembly intermediates of cytochrome b (Cytb), a central subunit of complex III. The predicted structure of the first assembly intermediate suggests how the binding of Cytb to the assembly factor Cbp3‐Cbp6 imposes an open configuration to facilitate the acquisition of its heme cofactors. Moreover, structure predictions of the second intermediate indicate how hemes get stabilized by binding of the assembly factor Cbp4, with a concomitant weakening of the contact between Cbp3‐Cbp6 and Cytb, preparing for the release of the fully hemylated protein from the assembly factors.

Funder

Knut och Alice Wallenbergs Stiftelse

Vetenskapsrådet

Publisher

Wiley

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