3jbn | pdb_00003jbn

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Cryo-electron microscopy reconstruction of the Plasmodium falciparum 80S ribosome bound to P-tRNA

spinqualitylabelsall models 3jbn, resolution 4.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3jbn is a 78 chain structure with sequence from Escherichia coli and Plasmodium falciparum 3d7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: UNK Related: 3jbo, 3jbp Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Warning: this is a large structure, and loading might take a long time or not happen at all. Function [RSSA_PLAF7] Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits (By similarity). [C0H4L5_PLAF7] Binds to the 23S rRNA (By similarity).[RuleBase:RU000576] Publication Abstract from PubMed Plasmodium falciparum, the mosquito-transmitted Apicomplexan parasite, causes the most severe form of human malaria. In the asexual blood-stage, the parasite resides within erythrocytes where it proliferates, multiplies and finally spreads to new erythrocytes. Development of drugs targeting the ribosome, the site of protein synthesis, requires specific knowledge of its structure and work cycle, and, critically, the ways they differ from those in the human host. Here, we present five cryo-electron microscopy (cryo-EM) reconstructions of ribosomes purified from P. falciparum blood-stage schizonts at sub-nanometer resolution. Atomic models were built from these density maps by flexible fitting. Significantly, our study has taken advantage of new capabilities of cryo-EM, in visualizing several structures co-existing in the sample at once, at a resolution sufficient for building atomic models. We have discovered structural and dynamic features that differentiate the ribosomes of P. falciparum from those of mammalian system. Prompted by the absence of RACK1 on the ribosome in our and an earlier study we confirmed that RACK1 does not specifically co-purify with the 80S fraction in schizonts. More extensive studies, using cryo-EM methodology, of translation in the parasite will provide structural knowledge that may lead to development of novel anti-malarials. Dynamical features of the Plasmodium falciparum ribosome during translation.,Sun M, Li W, Blomqvist K, Das S, Hashem Y, Dvorin JD, Frank J Nucleic Acids Res. 2015 Oct 1. pii: gkv991. PMID:26432834 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also TRNA

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