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  Entropic contribution of elongation factor P to proline positioning at the catalytic center of the ribosome.

Dörfel, L. K., Wohlgemuth, I., Kubyshkin, V., Starosta, A. L., Wilson, D. N., Budisa, N., et al. (2015). Entropic contribution of elongation factor P to proline positioning at the catalytic center of the ribosome. Journal of the American Chemical Society, 137(40), 12997-13006. doi:10.1021/jacs.5b07427.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-E3C4-7 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-6056-4
Genre: Journal Article

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 Creators:
Dörfel, L. K.1, Author              
Wohlgemuth, I.1, Author              
Kubyshkin, V., Author
Starosta, A. L., Author
Wilson, D. N., Author
Budisa, N., Author
Rodnina, M. V.1, Author              
Affiliations:
1Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578598              

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 Abstract: The peptide bond formation with the amino acid proline (Pro) on the ribosome is slow, resulting in translational stalling when several Pro have to be incorporated into the peptide. Stalling at poly-Pro motifs is alleviated by the elongation factor P (EF-P). Here we investigate why Pro is a poor substrate and how EF-P catalyzes the reaction. Linear free energy relationships of the reaction on the ribosome and in solution using 12 different Pro analogues suggest that the positioning of Pro-tRNA in the peptidyl transferase center is the major determinant for the slow reaction. With any Pro analogue tested, EF-P decreases the activation energy of the reaction by an almost uniform value of 2.5 kcal/mol. The main source of catalysis is the favorable entropy change brought about by EF-P. Thus, EF-P acts by entropic steering of Pro-tRNA toward a catalytically productive orientation in the peptidyl transferase center of the ribosome.

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Language(s): eng - English
 Dates: 2015-09-182015-10-14
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1021/jacs.5b07427
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Title: Journal of the American Chemical Society
Source Genre: Journal
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Pages: - Volume / Issue: 137 (40) Sequence Number: - Start / End Page: 12997 - 13006 Identifier: -