Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins

Article Abstract:

A 2.7-Angstrom crystal structure of Escherichia coli trigger factor, the best-characterized chaperone, together with the structure of its ribosome-binding domain in complex with the Haloarcula marismortui large ribosomal subunit is presented. The trigger factor projects the extended domains over the exit of the ribosomal tunnel from its attachment point on the ribosome creating a protected folding space where nascent polypeptides may be shielded from proteases and aggregation.

Protein synthesis, Protein binding, Protein biosynthesis, Polypeptides

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Placement of protein and RNA structures into a 5 A-resolution map of the 50S ribosomal subunit

Article Abstract:

An electron-density map of the large 50S ribosomal subunit from the bacterium Haloarcular marismortui bacterium has been calculated at 5.0 A resolution. Phases were derived from heavy-atom derivatives, intercrystal density averaging and density-modification methods. Over 300 base pairs of A-form RNA duplex were fitted into the map. A polypeptide exit channel was marked by tungsten cluster compounds bound in a heavy-atom-derivatized crystal.

Ribosomes

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Crystal structure of the transfer-RNA domain of transfer-messenger RNA in complex with SmpB

Article Abstract:

The 3.2-A-resolution structure of the tRNA-like domain of tmRNA (tmRNA delta) in complex with small protein B (SmpB), a protein essential for biological functions of tmRNA, is reported. The findings indicate that flexible RNA molecule adopts an open L-shaped conformation and SmpB binds to its elbow region, stabilizing the single-stranded D-loop in an extended conformation.

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