Affinage · Plasmodium

PF3D7_1431700

60S ribosomal protein L14, putative

Annotated
2026-09-08
5 papers in source corpus 4 papers cited in narrative 4 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PF3D7_1431700 (L14) is a structural component of the large (60S) subunit of the Plasmodium falciparum 80S ribosome, resolved as part of the assembled particle in successive cryo-EM structures of the intact ribosome (PMID:24913268, PMID:26432834). It is present within the 60S subunit of actively translating ribosomes purified from blood-stage schizonts and of drug-bound complexes, and in situ cryo-electron tomography places L14 within the 60S subunit of the native ribosome as it operates during translation elongation inside infected erythrocytes (PMID:26432834, PMID:28288098, PMID:40825879). Beyond this membership in the 60S subunit of the translating ribosome, no specific catalytic activity or direct binding partner of L14 itself has been characterized in the available corpus.

Mechanistic history

Synthesis pass · year-by-year structured walk · 4 steps
  1. 2014 Medium

    Whether L14 is a constituent of the P. falciparum ribosome was resolved by the first high-resolution structure of the intact 80S particle, establishing it as a 60S subunit component.

    Evidence cryo-EM structure of the emetine-bound P. falciparum 80S ribosome at 3.2 Å

    PMID:24913268

    Open questions at the time
    • no functional experiment targeting L14 itself
    • no direct binding partner of L14 defined beyond the complex
    • no catalytic role assigned
  2. 2015 Medium

    Whether L14's placement held in ribosomes engaged in active translation was addressed by reconstructions from blood-stage schizonts, confirming it as a structural constituent of the translating 60S subunit.

    Evidence sub-nanometer cryo-EM with flexible fitting of atomic models from schizont-purified ribosomes

    PMID:26432834

    Open questions at the time
    • no assembly or stability role for L14 tested
    • does not define L14 interactions within the subunit
  3. 2017 Medium

    The persistence of L14 as a 60S component in a drug-bound ribosome was confirmed, though the study's functional focus was the mefloquine-binding GTPase-associated centre rather than L14.

    Evidence cryo-EM at 3.2 Å with site-directed mutagenesis of mefloquine-binding residues

    PMID:28288098

    Open questions at the time
    • mutagenesis targeted drug-binding residues, not L14
    • no direct link between L14 and drug binding
  4. 2025 Medium

    Whether L14's structural placement holds within the native cellular ribosome was addressed by in situ cryo-ET, positioning L14 in the 60S subunit of ribosomes actively translating inside infected erythrocytes.

    Evidence in situ cryo-electron tomography of P. falciparum-infected human erythrocytes, eight structures of translating states

    PMID:40825879

    Open questions at the time
    • no functional experiment on L14 itself
    • role of L14 in elongation dynamics not isolated

Open questions

Synthesis pass · forward-looking unresolved questions
  • Whether L14 has any function beyond its structural membership in the 60S subunit — catalytic activity, direct binding partners, or a role in ribosome assembly — remains unaddressed.
  • no gene-specific knockdown or knockout phenotype
  • no direct L14 interaction mapping
  • no catalytic function defined

Mechanism profile

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

Evidence

Reading pass · 4 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2014 The cryo-EM structure of the P. falciparum 80S ribosome at 3.2 Å resolution was solved with emetine bound, revealing L14 (PF3D7_1431700) as a component of the large (60S) ribosomal subunit within the assembled 80S complex. cryo-EM structure determination at 3.2 Å resolution eLife Medium 24913268
2015 Sub-nanometer cryo-EM reconstructions of ribosomes purified from P. falciparum blood-stage schizonts, with atomic model building by flexible fitting, confirm L14 (PF3D7_1431700) as a structural constituent of the 60S subunit of the actively translating 80S ribosome. cryo-EM with flexible fitting of atomic models from density maps Nucleic acids research Medium 26432834
2017 A 3.2 Å cryo-EM structure of the P. falciparum 80S ribosome with mefloquine bound to the GTPase-associated centre further establishes L14 (PF3D7_1431700) as a structural component of the 60S ribosomal subunit within the drug-bound complex. cryo-EM structure determination at 3.2 Å; site-directed mutagenesis of binding residues Nature microbiology Medium 28288098
2025 In situ cryo-electron tomography of P. falciparum-infected erythrocytes determined eight high-resolution structures of the native malarial ribosome in actively translating states, placing L14 (PF3D7_1431700) within the 60S subunit of the ribosome as it operates inside the native cellular context during translation elongation. 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