A 9 Angstrom resolution x-ray crystallographic map of a large ribosomal subunit

Article Abstract:

An x-ray crystallographic map showing the electron density features of the large ribosomal unit of Haloarcula marismortui was constructed at resolutions between 20 Angstroms and nine Angstroms. Comparisons reveal similarities with reconstructions made from electron microscopic (EM) images. In addition, molecular replacement procedures placed EM reconstructions of the ribosomal unit in the crystal unit cell of the H. marismortui. The resulting electron density was also found to diminish at resolutions higher than 9-10 Angstroms.

Analysis, Usage, Bacterial genetics, Proteins, Protein synthesis, X-ray crystallography

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Cryo-EM visualization of a viral internal ribosome entry site bound to human ribosomes: the IRES functions as an RNA-based translation factor

Article Abstract:

The molecular mechanism by which the cricket paralysis virus (CrPV) internal ribosome entry sites (IRES) recruits the ribosome is investigated by generating 3D reconstructions of the CrPV IRES bound to human ribosomal particles using single- particle cryo-EM. It was observed that CrPV IRES binding at components of the ribosomal A, P, and E sites actively manipulates the ribosome by inducing conformational changes and it is proposed that CrPV-like IRES elements are RNA-based translation factors.

RNA, Genetic translation, Translation (Genetics)

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Structures of MLS(sub B)K antibiotics bound to mutated large ribosomal subunits provide a structural explanation for resistance

Article Abstract:

A study is carried out on the crystal structures of H. marismortui large ribosomal subunits that contain the mutation G2099A (A2058 in E. Coli) that is bound with erythromycin, azithromycin, clindamycin, virginiamycin S, and telithromycin. This study gives a detailed explanation why eubacterial ribosomes containing the mutation A2058G are resistant to them.

Gene mutations, Gene mutation, Genetic aspects, Halophilic bacteria, Cell anatomy, Halophiles

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