Affinage · Plasmodium

PF3D7_1351400

60S ribosomal protein L17, putative

Annotated
2026-09-08
5 papers in source corpus 2 papers cited in narrative 2 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PF3D7_1351400 (L17) is a structural component of the large (60S) subunit of the Plasmodium falciparum cytoplasmic 80S ribosome, as established by cryo-EM of the intact ribosome (PMID:24913268) and confirmed within the native, actively translating machinery by in situ cryo-electron tomography inside infected erythrocytes (PMID:40825879). Beyond its membership in the 60S subunit, no enzymatic activity, binding partners, post-translational modifications, or functional role specific to L17 has been characterized in the available corpus.

Mechanistic history

Synthesis pass · year-by-year structured walk · 2 steps
  1. 2014 Medium

    Whether PF3D7_1351400 is part of the parasite's ribosome was resolved by placing it as a structural constituent of the 60S subunit within the assembled 80S ribosome.

    Evidence Cryo-EM structure determination of the P. falciparum 80S ribosome at 3.2 Å resolution

    PMID:24913268

    Open questions at the time
    • Membership is inferred from the structural map; no mutagenesis or functional assay specific to L17
    • No enzymatic activity or binding partner beyond the ribosome defined
    • Role in ribosome assembly or translation not tested
  2. 2025 Medium

    Whether L17's ribosomal placement holds in the native cellular context, rather than only in purified particles, was addressed by resolving the ribosome in actively translating states inside intact parasites.

    Evidence In situ cryo-electron tomography of the native ribosome inside P. falciparum-infected human erythrocytes, yielding eight translating-state structures

    PMID:40825879

    Open questions at the time
    • Structural membership is the only finding attributable to L17; no functional role assigned
    • No evidence for regulation, modification, or extra-ribosomal moonlighting function
    • Contribution of L17 to specific translational states not dissected

Open questions

Synthesis pass · forward-looking unresolved questions
  • What functional or regulatory role L17 plays beyond being a structural subunit of the 60S ribosome remains unknown.
  • No gene-specific mutagenesis, knockdown, or depletion phenotype reported
  • No binding partners outside the ribosome, no post-translational modifications identified
  • No test of essentiality or druggability specific to L17

Mechanism profile

Synthesis pass · controlled-vocabulary classification
Complex memberships
60S large ribosomal subunit of the P. falciparum cytoplasmic 80S ribosome

Evidence

Reading pass · 2 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2014 Cryo-EM structure of the P. falciparum 80S ribosome at 3.2 Å resolution established that PF3D7_1351400 (60S ribosomal protein L17) is a structural component of the large (60S) ribosomal subunit of the cytoplasmic 80S ribosome. Cryo-EM structure determination at 3.2 Å resolution eLife Medium 24913268
2025 In situ cryo-electron tomography of P. falciparum-infected erythrocytes resolved eight high-resolution structures of the native malarial ribosome in actively translating states, confirming that PF3D7_1351400 (L17) is a constituent of the 60S subunit within the native cellular translation machinery. In situ cryo-electron tomography inside P. falciparum-infected human erythrocytes Nature structural & molecular biology Medium 40825879

Source papers

Stage 0 corpus · 5 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2014 Cryo-EM structure of the Plasmodium falciparum 80S ribosome bound to the anti-protozoan drug emetine. eLife 272 24913268
2017 Mefloquine targets the Plasmodium falciparum 80S ribosome to inhibit protein synthesis. Nature microbiology 136 28288098
2015 Dynamical features of the Plasmodium falciparum ribosome during translation. Nucleic acids research 45 26432834
2025 Integrated structural biology of the native malarial translation machinery and its inhibition by an antimalarial drug. Nature structural & molecular biology 7 40825879
2025 Antimalarial drug artemisinin stabilizes PfRACK1 binding to the ribosome. Structure (London, England : 1993) 3 40480224