- EMDB-50470: SSU(body) structure derived from the SSU sample of the mitoriboso... -
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Basic information
Entry
Database: EMDB / ID: EMD-50470
Title
SSU(body) structure derived from the SSU sample of the mitoribosome from T. gondii.
Map data
Sample
Complex: LSU structure derived from the LSU sample of the mitoribosome from T. gondii.
Protein or peptide: x 43 types
RNA: x 23 types
Keywords
Complex / translation / rRNA / RIBOSOME
Function / homology
Function and homology information
hydro-lyase activity / mitochondrial small ribosomal subunit / mitochondrial translation / fatty acid metabolic process / isomerase activity / small ribosomal subunit / small ribosomal subunit rRNA binding / ribosome / structural constituent of ribosome / translation ...hydro-lyase activity / mitochondrial small ribosomal subunit / mitochondrial translation / fatty acid metabolic process / isomerase activity / small ribosomal subunit / small ribosomal subunit rRNA binding / ribosome / structural constituent of ribosome / translation / ribonucleoprotein complex / mitochondrion / DNA binding / RNA binding / cytoplasm Similarity search - Function
: / Enoyl-CoA hydratase/isomerase domain / Enoyl-CoA hydratase/isomerase / Acylphosphatase-like domain / Acylphosphatase-like domain profile. / Double stranded RNA-binding domain (dsRBD) profile. / Double-stranded RNA-binding domain / ClpP/crotonase-like domain superfamily / Homeobox-like domain superfamily / Ribosomal protein S6, plastid/chloroplast ...: / Enoyl-CoA hydratase/isomerase domain / Enoyl-CoA hydratase/isomerase / Acylphosphatase-like domain / Acylphosphatase-like domain profile. / Double stranded RNA-binding domain (dsRBD) profile. / Double-stranded RNA-binding domain / ClpP/crotonase-like domain superfamily / Homeobox-like domain superfamily / Ribosomal protein S6, plastid/chloroplast / Ribosomal protein S16 / Ribosomal protein S16 domain superfamily / Ribosomal protein S16 / Ribosomal protein S15, bacterial-type / Ribosomal protein S12, bacterial-type / Ribosomal protein S18 / Ribosomal protein S18 / Ribosomal protein S18 superfamily / Ribosomal protein S6 / Ribosomal protein S6 / Ribosomal protein S6 superfamily / Translation elongation factor EF1B/ribosomal protein S6 / S5 double stranded RNA-binding domain profile. / Ribosomal protein S5, N-terminal / Ribosomal protein S5, N-terminal domain / Ribosomal protein S8 / Ribosomal protein S8 superfamily / Ribosomal protein S8 / Ribosomal protein S12/S23 / Ribosomal protein S12/S23 / Ribosomal protein S17/S11 / Ribosomal protein S17 / Ribosomal protein S15 / Ribosomal_S15 / Ribosomal protein S15 / Ribosomal protein S11 superfamily / S15/NS1, RNA-binding / Macro domain / Macro domain profile. / Macro domain / Macro domain-like / Ribosomal protein S5 domain 2-type fold, subgroup / Ribosomal protein S5 domain 2-type fold / Nucleic acid-binding, OB-fold Similarity search - Domain/homology
Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Putative ribosomal protein S17 / Acylphosphatase-like domain-containing protein / Uncharacterized protein / Uncharacterized protein / Putative homeodomain containing protein / Uncharacterized protein / CHCH domain-containing protein ...Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Putative ribosomal protein S17 / Acylphosphatase-like domain-containing protein / Uncharacterized protein / Uncharacterized protein / Putative homeodomain containing protein / Uncharacterized protein / CHCH domain-containing protein / Putative 30S ribosomal protein S15 / Putative ribosomal protein S8 / Uncharacterized protein / Putative mitochondrial ribosomal protein s6-2 / DnaJ domain-containing protein / Putative 30S ribosomal protein S16 / Enoyl-CoA hydratase/isomerase family protein / 30S ribosomal protein S12, putative / Uncharacterized protein / Pentatricopeptide repeat domain-containing protein / 30S ribosomal protein S5, putative / Ribosomal protein S11, putative / Ribosomal protein S18, putative / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Macro domain-containing protein / RAP domain-containing protein Similarity search - Component
Biological species
Toxoplasma gondii (eukaryote)
Method
single particle reconstruction / cryo EM / Resolution: 3.29 Å
Journal: Nat Commun / Year: 2024 Title: Apicomplexan mitoribosome from highly fragmented rRNAs to a functional machine. Authors: Chaoyue Wang / Sari Kassem / Rafael Eduardo Oliveira Rocha / Pei Sun / Tan-Trung Nguyen / Joachim Kloehn / Xianyong Liu / Lorenzo Brusini / Alessandro Bonavoglia / Sramona Barua / Fanny ...Authors: Chaoyue Wang / Sari Kassem / Rafael Eduardo Oliveira Rocha / Pei Sun / Tan-Trung Nguyen / Joachim Kloehn / Xianyong Liu / Lorenzo Brusini / Alessandro Bonavoglia / Sramona Barua / Fanny Boissier / Mayara Lucia Del Cistia / Hongjuan Peng / Xinming Tang / Fujie Xie / Zixuan Wang / Oscar Vadas / Xun Suo / Yaser Hashem / Dominique Soldati-Favre / Yonggen Jia / Abstract: The phylum Apicomplexa comprises eukaryotic parasites that cause fatal diseases affecting millions of people and animals worldwide. Their mitochondrial genomes have been significantly reduced, ...The phylum Apicomplexa comprises eukaryotic parasites that cause fatal diseases affecting millions of people and animals worldwide. Their mitochondrial genomes have been significantly reduced, leaving only three protein-coding genes and highly fragmented mitoribosomal rRNAs, raising challenging questions about mitoribosome composition, assembly and structure. Our study reveals how Toxoplasma gondii assembles over 40 mt-rRNA fragments using exclusively nuclear-encoded mitoribosomal proteins and three lineage-specific families of RNA-binding proteins. Among these are four proteins from the Apetala2/Ethylene Response Factor (AP2/ERF) family, originally known as transcription factors in plants and Apicomplexa, now repurposed as essential mitoribosome components. Cryo-EM analysis of the mitoribosome structure demonstrates how these AP2 proteins function as RNA binders to maintain mitoribosome integrity. The mitoribosome is also decorated with members of lineage-specific RNA-binding proteins belonging to RAP (RNA-binding domain abundant in Apicomplexa) proteins and HPR (heptatricopeptide repeat) families, highlighting the unique adaptations of these parasites. Solving the molecular puzzle of apicomplexan mitoribosome could inform the development of therapeutic strategies targeting organellar translation.
Macromolecule #42: 30S ribosomal protein S5, putative
Macromolecule
Name: 30S ribosomal protein S5, putative / type: protein_or_peptide / ID: 42 Details: Right sequence (uniprot ID = S8F5G8): ...Details: Right sequence (uniprot ID = S8F5G8): MRCPLAPRRQRRLPRDSSSSVSLFLPHRGSLSLSSAFSPSFRRSPCPRSSPCLASSVPPSRLFSSASPNDSRLALKKPLSPSFSSPFAFSRYTRDPELRHLTSTSRVQAPLPLRRCAAPVASLASSPCLSSSRASSASLSPCSLASLGSRSSPFCGGSRRGGERPPCERRASAGCGAAANSFSSAPRPSRLSPSSPFFPSGLGCSSSPAHRARVAGPRLPLRSAFVALFPGQPTRTLCFPAASSALSFSAQPSPPTASASSFQSPRRLHNSHQARVLRRRHVYRDKHLDHVPTERARQLAEQRSAFELPRGTGEPLQGGSRFPGGVMAPHLRVKLEKEKFLRDCMREQENLAALFTETEKETLLGRRGDSRESHEEEPATREAEKQTSEGGKSDEAGKDGGKQEDKQGAAPFGRKLQELESFVGSALRTYRLLRPHALPFYKEDSLLSMQSKLNEATLKHSPLVHDLVELKKRNLSVPSDLLPPDFNALQFSLPVVSARGFLLALSAAANSVAEDLEFLCRRLSVPNLPHPTHPFRLKLLLDALFESFKLRKDPHYAHDWAQRNWPRLQAAMPEPLSELSADSVGLWLKAHLERVIENQRGRHADGRGRLLAQKFPLKSDEEDLYSLADDFIFDHEIVDEQFCDERLSQFPIDKAGELFRRVADFFGLTKGPQPAVNDAVVAQFQNLVYTLDEIGLSNWMKMDTREIEEFLPEGDPPSFAASQQDLDAARLLLKAAARGKANLLDFEALDPYKLLHGFDFKTVQEELATLPPNPFLTDADIDELFDITTAAVSMNQSEVAPSASLRNFKAKFGRTPLEALLDSEEKFLTSAGPVDWLKDEDENGEAFVSWRWKRPAQTVYDAEKGMFVREREGVDPLIKLHELRQTLLSVSRMMSMNKQGRVYYFRAIVAVGNGRGLFGIGIAFGPSPKEARSNAALAAIQNLDHIDFDVGRTLTTPVHGSEYSAHVKIVPRPLGKGLKSNLRYLPLLYLMGIDNCRVSFYGPSASARWFTRAKALKRALEQLQSRRTLANATGQKYDLLVAPGEHWMHWPDRWFRPISTEYARMLERIKKKRPPSYRRGFRAAIDEVIPEEIRPEFTPYTWKSPLQKWAEELKRKRLTSHNVYETEVFLHPPAQSSSPS Number of copies: 1 / Enantiomer: LEVO
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