Thermodynamics of the GTP-GDP-operated Conformational Switch of Selenocysteine-specific Translation Factor SelB. Alena Paleskava, Andrey L. Konevega and Marina V. Rodnina . The Journal of Biological Chemistry, 287, 27906-27912 (2012).  doi: 10.1074/jbc.M112.366120  .

6.  Briefly summarize the main findings that clarify RelB function in a cell.

Answer: The data indicate that SelB can adopt three discrete conformations that are clearly distinct from each other: the apo form, which is the most open form of the protein, the closed GTP-bound form; and the GDP-bound form, which is the intermediate between the apo form and the GTP-bound form. Given the high concentration of GTP in the cell and the high rate of nucleotide binding to SelB, the apo form is most probably short lived and therefore unlikely to play a functional role, whereas the transition between the GTP to GDP form is essential for the function of SelB on the ribosome.  ITC analysis suggests that the GTP- and GDP-bound forms of SelB are different and that the factor is likely to follow the functional and structural cycle typical for many other GTPases

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