Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural insights into cauliflower mitoribosome in translation state and in association with a late assembly factor.
Journal, issue, pages	Nat Commun, Vol. 16, Issue 1, Page 10839, Year 2025
Publish date	Dec 2, 2025
Authors	Vasileios Skaltsogiannis / Philippe Wolff / Tan-Trung Nguyen / Nicolas Corre / David Pflieger / Todd Blevins / Yaser Hashem / Philippe Giegé / Florent Waltz /
PubMed Abstract	Ribosomes are key molecular machines that translate mRNA into proteins. Mitoribosomes are specific ribosomes found in mitochondria, which have been shown to be remarkably diverse across eukaryotic ...Ribosomes are key molecular machines that translate mRNA into proteins. Mitoribosomes are specific ribosomes found in mitochondria, which have been shown to be remarkably diverse across eukaryotic lineages. In plants, they possess unique features, including additional rRNA domains stabilized by plant-specific proteins. However, the structural specificities of plant mitoribosomes in translation state remained unknown. We used cryo-electron microscopy to provide a high-resolution structural characterization of the cauliflower mitoribosome, in translating and maturation states. The structure reveals the mitoribosome bound with a tRNA in the peptidyl site, along with a segment of mRNA and a nascent polypeptide. Moreover, using structural data, nanopore sequencing and mass spectrometry, we identify a set of 19 ribosomal RNA modifications. Additionally, we observe a late assembly intermediate of the small ribosomal subunit, in complex with the RsgA assembly factor. This reveals how a plant-specific extension of RsgA blocks the mRNA channel to prevent premature mRNA association before complete small subunit maturation. Our findings elucidate key aspects of translation in angiosperm plant mitochondria, revealing its distinct features compared to other eukaryotic lineages.
External links	Nat Commun / PubMed:41330901 / PubMed Central
Methods	EM (single particle)
Resolution	1.99 - 4.32 Å
Structure data	50011 9evs EMDB-50011, PDB-9evs: Structure of the flowering plant mitoribosome with P-site tRNA Method: EM (single particle) / Resolution: 3.05 Å EMDB-50012: Structure of the flowering plant mitoribosome with P-site tRNA, large subunit focused Method: EM (single particle) / Resolution: 2.95 Å EMDB-50013: Structure of the flowering plant mitoribosome with P-site tRNA, small subunit focused Method: EM (single particle) / Resolution: 3.08 Å EMDB-50015: Structure of the small subunit of the flowering plant mitoribosome with the maturation factor RsgA, head focused Method: EM (single particle) / Resolution: 2.07 Å EMDB-50016: Structure of the small subunit of the flowering plant mitoribosome with the maturation factor RsgA, RsgA focused Method: EM (single particle) / Resolution: 2.07 Å EMDB-50017: Structure of the small subunit of the flowering plant mitoribosome with the maturation factor RsgA, body focused Method: EM (single particle) / Resolution: 2.17 Å EMDB-51703: High resolution structure of B. oleracea mitoribosome - unfocused Method: EM (single particle) / Resolution: 2.11 Å EMDB-51704: High resolution structure of B. oleracea mitoribosome - Small subunit body focused Method: EM (single particle) / Resolution: 2.25 Å EMDB-51705: High resolution structure of B. oleracea mitoribosome - Small subunit head focus Method: EM (single particle) / Resolution: 2.24 Å EMDB-51706: High resolution structure of B. oleracea mitoribosome - Small subunit head S3 area focus Method: EM (single particle) / Resolution: 2.41 Å EMDB-51707: High resolution structure of B. oleracea mitoribosome - Small subunit foot rPPR10 focus Method: EM (single particle) / Resolution: 2.76 Å EMDB-51708: High resolution structure of B. oleracea mitoribosome - Small subunit foot rPPR1 focus Method: EM (single particle) / Resolution: 2.7 Å EMDB-51709: High resolution structure of B. oleracea mitoribosome - Small subunit body protuberance focus Method: EM (single particle) / Resolution: 2.58 Å EMDB-51710: High resolution structure of B. oleracea mitoribosome - Large subunit focus Method: EM (single particle) / Resolution: 1.99 Å EMDB-51711: High resolution structure of B. oleracea mitoribosome - Large subunit Central Protuberance focus Method: EM (single particle) / Resolution: 2.09 Å EMDB-51712: High resolution structure of B. oleracea mitoribosome - Large subunit L7/12 stalk focus Method: EM (single particle) / Resolution: 2.85 Å EMDB-51713: High resolution structure of B. oleracea mitoribosome - Large subunit back protuberance focus Method: EM (single particle) / Resolution: 2.53 Å EMDB-51714: High resolution structure of B. oleracea mitoribosome - Large subunit rPPR5 focus Method: EM (single particle) / Resolution: 2.09 Å EMDB-51715: High resolution structure of B. oleracea mitoribosome - Small subunit head extension base focus Method: EM (single particle) / Resolution: 3.43 Å EMDB-51716: High resolution structure of B. oleracea mitoribosome - Small subunit head extension core focus Method: EM (single particle) / Resolution: 4.04 Å EMDB-51717: High resolution structure of B. oleracea mitoribosome - Small subunit head extension tip focus Method: EM (single particle) / Resolution: 4.32 Å 51718 9gyt EMDB-51718, PDB-9gyt: High resolution structure of B. oleracea mitoribosome Method: EM (single particle) / Resolution: 2.11 Å
Chemicals	ChemComp-MG: Unknown entry ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM ChemComp-CLM: CHLORAMPHENICOL / antibioticYM ChemComp-K: Unknown entry ChemComp-ZN: Unknown entry ChemComp-HOH: WATER
Source	brassica oleracea var. botrytis (cauliflower) brassica oleracea var. oleracea (plant) arabidopsis thaliana (thale cress)
Keywords	RIBOSOME / Mitochondria / tRNA / mitoribosome / plant / assembly factor