A protein-making motor protein

Article Abstract:

The ribosomal protein that catalyzes the mRNA translocation step, or the elongation factor G (EF-G), does not simply bind and dissociate once per notch but is an authentic motor protein. It is able to amplify and harness the shifts in the global shape of the molecule so as to step itself along 'tracks' such as actin, microtubules and DNA. Experimental data also reveals that the distal domains 4 and 5 of EF-G are of the same shape as the tRNA binding partner of EF-Tu. The transition from GTP to GDP-binding in the EF-Tu and the mimetic domain 4 of EF-G act as mechanical manipulators.

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The structure of ribosomal protein S5 reveals sites of interaction with 16S rRNA

Article Abstract:

S5, a ribosomal protein, has mutations that enable the molecule to interact with ribosomal RNA and so help the ribosome to translate the genetic code into protein molecules. S5 is the first ribosomal protein whose structure has been determined in detail: it has a molecular mass of 17,500, is well conserved in all organisms and has separate alpha/beta domains. Furthermore, S5 has structural discrepancies when compared to models of the 30S subunit.

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A mechanical explanation of RNA pseudoknot function in programmed ribosomal frameshifting

Article Abstract:

The observation of a ribosome-mRNA pseudoknot complex that is stalled in the process of - 1 frameshifting was described. It was found that the structural changes provide a mechanical explanation of how the pseudoknot manipulates the ribosome into a different reading frame.

Science & research, Structure-activity relationships (Biochemistry), Structure

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