Ribosomal protein S12 / Ribosomal protein S12 / Nucleoid-associated protein YbaB-like domain superfamily / : / Protein kinase A anchor protein, nuclear localisation signal domain / AKAP7 2'5' RNA ligase-like domain / Probable Zinc-ribbon domain / Probable Zinc-ribbon domain / : / TRAPP I complex, subunit 5 ...Ribosomal protein S12 / Ribosomal protein S12 / Nucleoid-associated protein YbaB-like domain superfamily / : / Protein kinase A anchor protein, nuclear localisation signal domain / AKAP7 2'5' RNA ligase-like domain / Probable Zinc-ribbon domain / Probable Zinc-ribbon domain / : / TRAPP I complex, subunit 5 / Enoyl-CoA hydratase/isomerase, HIBYL-CoA-H type / Enoyl-CoA hydratase/isomerase domain / Enoyl-CoA hydratase/isomerase / Protein Fyv4 / IGR protein motif / IGR / Cyclic phosphodiesterase / Ribosomal protein S23/S29, mitochondrial / Mitochondrial ribosomal death-associated protein 3 / Rhodanese-like domain / LysM domain / Rhodanese domain profile. / Rhodanese-like domain superfamily / LysM domain / Rhodanese-like domain / Manganese/iron superoxide dismutase, C-terminal / Manganese/iron superoxide dismutase, C-terminal domain superfamily / Manganese/iron superoxide dismutase, N-terminal domain superfamily / Iron/manganese superoxide dismutases, C-terminal domain / ClpP/crotonase-like domain superfamily / Ribosomal protein S6 superfamily / Translation elongation factor EF1B/ribosomal protein S6 / Ribosomal protein S18 superfamily / Ribosomal protein S5, C-terminal / Ribosomal protein S5, C-terminal domain / Ribosomal protein S8 / Ribosomal protein S8 superfamily / Ribosomal protein S8 / Tetratricopeptide-like helical domain superfamily / Ribosomal protein S9 / Ribosomal protein S9/S16 / Ribosomal protein S17/S11 / Ribosomal protein S17 / Ribosomal protein S11 superfamily / S15/NS1, RNA-binding / Ribosomal protein S5 domain 2-type fold, subgroup / Ubiquitin-like domain superfamily / Ribosomal protein S5 domain 2-type fold / Nucleic acid-binding, OB-fold Similarity search - Domain/homology
GUANOSINE-5'-TRIPHOSPHATE / URIDINE 5'-TRIPHOSPHATE / RNA / RNA (> 10) / RNA (> 100) / RNA (> 1000) / Ribosome protein S12 / 30S Ribosomal protein S17-like protein / Superoxide dismutase, putative / Manganese/iron superoxide dismutase C-terminal domain-containing protein ...GUANOSINE-5'-TRIPHOSPHATE / URIDINE 5'-TRIPHOSPHATE / RNA / RNA (> 10) / RNA (> 100) / RNA (> 1000) / Ribosome protein S12 / 30S Ribosomal protein S17-like protein / Superoxide dismutase, putative / Manganese/iron superoxide dismutase C-terminal domain-containing protein / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Trans-sialidase / Uncharacterized protein / Uncharacterized protein / A-kinase anchor protein 7-like phosphoesterase domain-containing protein / 3-hydroxyisobutyryl-CoA hydrolase / LysM domain-containing protein / HMG box domain-containing protein / Ribosomal protein S9 / Mitochondrial SSU ribosomal protein / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Mitochondrial RNA binding protein 1 / Uncharacterized protein / Small ribosomal subunit protein mS29 / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Rhodanese domain-containing protein / 30S ribosomal protein S8 / Small ribosomal subunit protein uS5 C-terminal domain-containing protein / Uncharacterized protein / Small ribosomal subunit protein mS41 / Opioid growth factor receptor (OGFr) conserved domain-containing protein / Probable Zinc-ribbon domain-containing protein / Trafficking protein particle complex subunit / Ubiquitin-like domain-containing protein / Mitochondrial SSU ribosomal protein / Mitochondrial ribosomal protein S18 / Chromosome passenger complex (CPC) protein INCENP N terminal Similarity search - Component
Biological species
Trypanosoma cruzi (eukaryote)
Method
ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.5 Å
Journal: Proc Natl Acad Sci U S A / Year: 2020 Title: Structure of the mature kinetoplastids mitoribosome and insights into its large subunit biogenesis. Authors: Heddy Soufari / Florent Waltz / Camila Parrot / Stéphanie Durrieu-Gaillard / Anthony Bochler / Lauriane Kuhn / Marie Sissler / Yaser Hashem / Abstract: Kinetoplastids are unicellular eukaryotic parasites responsible for such human pathologies as Chagas disease, sleeping sickness, and leishmaniasis. They have a single large mitochondrion, essential ...Kinetoplastids are unicellular eukaryotic parasites responsible for such human pathologies as Chagas disease, sleeping sickness, and leishmaniasis. They have a single large mitochondrion, essential for the parasite survival. In kinetoplastid mitochondria, most of the molecular machineries and gene expression processes have significantly diverged and specialized, with an extreme example being their mitochondrial ribosomes. These large complexes are in charge of translating the few essential mRNAs encoded by mitochondrial genomes. Structural studies performed in already highlighted the numerous peculiarities of these mitoribosomes and the maturation of their small subunit. However, several important aspects mainly related to the large subunit (LSU) remain elusive, such as the structure and maturation of its ribosomal RNA. Here we present a cryo-electron microscopy study of the protozoans and mitoribosomes. For both species, we obtained the structure of their mature mitoribosomes, complete rRNA of the LSU, as well as previously unidentified ribosomal proteins. In addition, we introduce the structure of an LSU assembly intermediate in the presence of 16 identified maturation factors. These maturation factors act on both the intersubunit and the solvent sides of the LSU, where they refold and chemically modify the rRNA and prevent early translation before full maturation of the LSU.
In the structure databanks used in Yorodumi, some data are registered as the other names, "COVID-19 virus" and "2019-nCoV". Here are the details of the virus and the list of structure data.
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)
EMDB accession codes are about to change! (news from PDBe EMDB page)
The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
The EM Navigator/Yorodumi systems omit the EMD- prefix.
Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator
Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.
Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi