{"entity": "researcher", "timestamp": "2026-08-20T20:45:30.049Z", "family": "Ott", "given": "Martin", "initials": "M", "orcid": "0000-0001-6367-3091", "affiliations": ["Department of Biochemistry and Biophysics, Stockholm University SE-10691 Stockholm, Sweden martin.ott@dbb.su.se."], "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/researcher/3a4e515dde6d415cb0b0b4877cc7207a.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/researcher/3a4e515dde6d415cb0b0b4877cc7207a"}}, "publications": [{"entity": "publication", "iuid": "9ab5835c732a4b7d97d4b021c093454b", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/9ab5835c732a4b7d97d4b021c093454b.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/9ab5835c732a4b7d97d4b021c093454b"}}, "title": "Structural basis for the interaction of the chaperone Cbp3 with newly synthesized cytochrome b during mitochondrial respiratory chain assembly.", "authors": [{"family": "Ndi", "given": "Mama", "initials": "M"}, {"family": "Masuyer", "given": "Geoffrey", "initials": "G", "orcid": "0000-0002-9527-2310", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/c62ba219d3e34662aaa458dbd361cf31.json"}}, {"family": "Dawitz", "given": "Hannah", "initials": "H"}, {"family": "Carlstr\u00f6m", "given": "Andreas", "initials": "A"}, {"family": "Michel", "given": "Mirco", "initials": "M"}, {"family": "Elofsson", "given": "Arne", "initials": "A"}, {"family": "Rapp", "given": "Mikaela", "initials": "M"}, {"family": "Stenmark", "given": "P\u00e5l", "initials": "P", "orcid": "0000-0003-4777-3417", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/9791bc0d7463417899d6953b5ca1bac3.json"}}, {"family": "Ott", "given": "Martin", "initials": "M", "orcid": "0000-0001-6367-3091", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/3a4e515dde6d415cb0b0b4877cc7207a.json"}}], "type": "journal article", "published": "2019-11-08", "journal": {"title": "J Biol Chem", "issn": "1083-351X", "volume": "294", "issue": "45", "pages": "16663-16671", "issn-l": "0021-9258"}, "abstract": "Assembly of the mitochondrial respiratory chain requires the coordinated synthesis of mitochondrial and nuclear encoded subunits, redox co-factor acquisition, and correct joining of the subunits to form functional complexes. The conserved Cbp3-Cbp6 chaperone complex binds newly synthesized cytochrome b and supports the ordered acquisition of the heme co-factors. Moreover, it functions as a translational activator by interacting with the mitoribosome. Cbp3 consists of two distinct domains: an N-terminal domain present in mitochondrial Cbp3 homologs and a highly conserved C-terminal domain comprising a ubiquinol-cytochrome c chaperone region. Here, we solved the crystal structure of this C-terminal domain from a bacterial homolog at 1.4 \u00c5 resolution, revealing a unique all-helical fold. This structure allowed mapping of the interaction sites of yeast Cbp3 with Cbp6 and cytochrome b via site-specific photo-cross-linking. We propose that mitochondrial Cbp3 homologs carry an N-terminal extension that positions the conserved C-terminal domain at the ribosomal tunnel exit for an efficient interaction with its substrate, the newly synthesized cytochrome b protein.", "doi": "10.1074/jbc.RA119.010483", "pmid": "31537648", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC6851329"}, {"db": "pii", "key": "S0021-9258(20)30513-5"}, {"db": "PDB", "key": "6GIQ"}, {"db": "PDB", "key": "5MRC"}, {"db": "PDB", "key": "6RWT"}], "notes": [], "created": "2026-08-20T09:32:17.818Z", "modified": "2026-08-20T09:32:17.966Z"}]}