{"entity": "researcher", "timestamp": "2026-08-07T19:16:37.985Z", "family": "Rathore", "given": "Sorbhi", "initials": "S", "orcid": "0000-0001-9178-1006", "affiliations": ["Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden."], "links": {"self": {"href": "https://publications.scilifelab.se/researcher/5c2293f9f60f44cfa47f1e3691c1309d.json"}, "display": {"href": "https://publications.scilifelab.se/researcher/5c2293f9f60f44cfa47f1e3691c1309d"}}, "publications": [{"entity": "publication", "iuid": "92dba4d4ec6f45f9ad59022513e674eb", "links": {"self": {"href": "https://publications.scilifelab.se/publication/92dba4d4ec6f45f9ad59022513e674eb.json"}, "display": {"href": "https://publications.scilifelab.se/publication/92dba4d4ec6f45f9ad59022513e674eb"}}, "title": "Cryo-EM structure of the yeast respiratory supercomplex.", "authors": [{"family": "Rathore", "given": "Sorbhi", "initials": "S", "orcid": "0000-0001-9178-1006", "researcher": {"href": "https://publications.scilifelab.se/researcher/5c2293f9f60f44cfa47f1e3691c1309d.json"}}, {"family": "Berndtsson", "given": "Jens", "initials": "J", "orcid": "0000-0001-6627-8134", "researcher": {"href": "https://publications.scilifelab.se/researcher/7620a5c7c0f245a28771d57d7179abbd.json"}}, {"family": "Marin-Buera", "given": "Lorena", "initials": "L"}, {"family": "Conrad", "given": "Julian", "initials": "J"}, {"family": "Carroni", "given": "Marta", "initials": "M", "orcid": "0000-0002-7697-6427", "researcher": {"href": "https://publications.scilifelab.se/researcher/e7f1bc1767024368abcb11a83184994a.json"}}, {"family": "Brzezinski", "given": "Peter", "initials": "P", "orcid": "0000-0003-3860-4988", "researcher": {"href": "https://publications.scilifelab.se/researcher/e3314030ecf94791a713a068d4926c20.json"}}, {"family": "Ott", "given": "Martin", "initials": "M", "orcid": "0000-0001-6367-3091", "researcher": {"href": "https://publications.scilifelab.se/researcher/b27b582dbd2a47bcbb0fb3194277902a.json"}}], "type": "journal article", "published": "2019-01-00", "journal": {"title": "Nat. Struct. Mol. Biol.", "issn": "1545-9985", "volume": "26", "issue": "1", "pages": "50-57", "issn-l": "1545-9985"}, "abstract": "Respiratory chain complexes execute energy conversion by connecting electron transport with proton translocation over the inner mitochondrial membrane to fuel ATP synthesis. Notably, these complexes form multi-enzyme assemblies known as respiratory supercomplexes. Here we used single-particle cryo-EM to determine the structures of the yeast mitochondrial respiratory supercomplexes III 2IV and III2IV2, at 3.2-\u00c5 and 3.5-\u00c5 resolutions, respectively. We revealed the overall architecture of the supercomplex, which deviates from the previously determined assemblies in mammals; obtained a near-atomic structure of the yeast complex IV; and identified the protein-protein and protein-lipid interactions implicated in supercomplex formation. Take together, our results demonstrate convergent evolution of supercomplexes in mitochondria that, while building similar assemblies, results in substantially different arrangements and structural solutions to support energy conversion.", "doi": "10.1038/s41594-018-0169-7", "pmid": "30598556", "labels": {"Cryo-EM": "Collaborative"}, "xrefs": [{"db": "pii", "key": "10.1038/s41594-018-0169-7"}], "notes": [], "created": "2019-01-03T16:38:40.124Z", "modified": "2021-06-21T13:49:53.118Z"}, {"entity": "publication", "iuid": "2169891b741d469abe009aa481604680", "links": {"self": {"href": "https://publications.scilifelab.se/publication/2169891b741d469abe009aa481604680.json"}, "display": {"href": "https://publications.scilifelab.se/publication/2169891b741d469abe009aa481604680"}}, "title": "Structures of the human mitochondrial ribosome in native states of assembly", "authors": [{"family": "Brown", "given": "Alan", "initials": "A", "orcid": "0000-0002-0021-0476", "researcher": {"href": "https://publications.scilifelab.se/researcher/2bb38a7f086247fdb2e2b3bfb80dae1e.json"}}, {"family": "Rathore", "given": "Sorbhi", "initials": "S", "orcid": "0000-0001-9178-1006", "researcher": {"href": "https://publications.scilifelab.se/researcher/5c2293f9f60f44cfa47f1e3691c1309d.json"}}, {"family": "Kimanius", "given": "Dari", "initials": "D", "orcid": "0000-0002-2662-6373", "researcher": {"href": "https://publications.scilifelab.se/researcher/df2317a49446495a8839262b9f58fe38.json"}}, {"family": "Aibara", "given": "Shintaro", "initials": "S", "orcid": "0000-0003-2221-482X", "researcher": {"href": "https://publications.scilifelab.se/researcher/d66746c4bec5414da78b2a325a13328f.json"}}, {"family": "Bai", "given": "Xiao chen", "initials": "Xc"}, {"family": "Rorbach", "given": "Joanna", "initials": "J", "orcid": "0000-0002-2891-2840", "researcher": {"href": "https://publications.scilifelab.se/researcher/a069374613a7403b818ce7ca400f3627.json"}}, {"family": "Amunts", "given": "Alexey", "initials": "A", "orcid": "0000-0002-5302-1740", "researcher": {"href": "https://publications.scilifelab.se/researcher/e7d0bf36ad1a47f5b5b88f78d1e15395.json"}}, {"family": "Ramakrishnan", "given": "V", "initials": "V", "orcid": "0000-0002-4699-2194", "researcher": {"href": "https://publications.scilifelab.se/researcher/9c59648b4e90409da2fcd0c4ae0355c6.json"}}], "type": "journal-article", "published": "2017-10-00", "journal": {"volume": "24", "issn": "1545-9993", "issue": "10", "pages": "866-869", "title": "Nat Struct Mol Biol", "issn-l": "1545-9985"}, "abstract": "Mammalian mitochondrial ribosomes (mitoribosomes) have less rRNA content and 36 additional proteins compared with the evolutionarily related bacterial ribosome. These differences make the assembly of mitoribosomes more complex than the assembly of bacterial ribosomes, but the molecular details of mitoribosomal biogenesis remain elusive. Here, we report the structures of two late-stage assembly intermediates of the human mitoribosomal large subunit (mt-LSU) isolated from a native pool within a human cell line and solved by cryo-EM to \u223c3-\u00c5 resolution. Comparison of the structures reveals insights into the timing of rRNA folding and protein incorporation during the final steps of ribosomal maturation and the evolutionary adaptations that are required to preserve biogenesis after the structural diversification of mitoribosomes. Furthermore, the structures redefine the ribosome silencing factor (RsfS) family as multifunctional biogenesis factors and identify two new assembly factors (L0R8F8 and mt-ACP) not previously implicated in mitoribosomal biogenesis.", "doi": "10.1038/nsmb.3464", "pmid": "28892042", "labels": {"Cryo-EM": "Service"}, "xrefs": [{"db": "mid", "key": "EMS73849"}, {"db": "pmc", "key": "PMC5633077"}, {"db": "pii", "key": "nsmb.3464"}], "notes": [], "created": "2017-10-16T16:18:18.520Z", "modified": "2023-12-04T10:11:28.653Z"}]}