PF3D7_1424400

PF3D7_1424400 (L7, 60S ribosomal protein L7-3, putative) is a structural component of the large (60S) subunit of the P. falciparum 80S ribosome, established by a 3.2 Å cryo-EM structure that resolved it as a constituent of the assembled ribosomal complex without assigning it a distinct catalytic or regulatory role beyond ribosome composition (PMID:24913268). Beyond this membership assignment, no experiment in the available corpus assigns a specific binding partner, substrate, or independent function to L7 itself; broader analyses of stage-specific ribosome heterogeneity and in situ translating-ribosome states place 60S large-subunit proteins of the L7 family in the malarial ribosome but do not characterize PF3D7_1424400 individually (PMID:37053161, PMID:40825879). No further mechanistic detail specific to L7 has been characterized in the available corpus.

1. 2014 Medium

   Whether L7/PF3D7_1424400 is part of the assembled P. falciparum ribosome was resolved by placing it structurally within the 60S large subunit, establishing it as a bona fide ribosomal protein of the parasite 80S complex.

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

   PMID:24913268

   Open questions at the time

   • No specific catalytic, regulatory, or binding function assigned to L7 beyond ribosome membership
   • No experiment directed at L7 itself; role inferred from the structural map
   • No interaction partners or substrates identified for L7 individually
2. 2023 Low

   Whether 60S ribosomal protein composition varies across the parasite life cycle was addressed by ribosome-heterogeneity analysis, placing L7-family large-subunit proteins in distinct stage-specific ribosome variants, though not resolving L7/PF3D7_1424400 individually.

   Evidence Structural and comparative analysis of stage-specific Plasmodium ribosomes (cryo-EM and proteomics)

   PMID:37053161

   Open questions at the time

   • Abstract does not specify L7/PF3D7_1424400 individually; membership in the heterogeneous pool is inferred from general L7-family findings
   • No functional consequence attributed to L7 in any specific life-cycle stage
   • Whether L7 itself is present or absent in specific variants is not established
3. 2025 Low

   Whether native, actively translating parasite ribosomes could be visualised in their cellular context was addressed by in situ cryo-electron tomography, resolving 60S large-subunit components including L7 as structural constituents of translating 80S ribosomes.

   Evidence In situ cryo-electron tomography of native ribosomes in P. falciparum-infected human erythrocytes, with perturbation by a Plasmodium-specific translation inhibitor

   PMID:40825879

   Open questions at the time

   • Abstract does not name L7/PF3D7_1424400 specifically; membership inferred from general 80S large-subunit analysis
   • No L7-specific contribution to elongation-factor binding or ribosome biogenesis established
   • The inhibitor effect is a ribosome-level observation, not an L7-directed one

• Whether L7/PF3D7_1424400 has any function beyond being a structural component of the 60S subunit — a specific role in assembly, translation regulation, or non-ribosomal activity — remains unaddressed.
• No experiment isolates or perturbs L7 individually
• No binding partners or substrates identified for L7 beyond the ribosome
• No genetic or biochemical test of L7 essentiality or function