Solution structures and backbone dynamics of the ribosomal protein S6 and its permutant P(54-55).

Protein Science : a Publication of the Protein Society
Anders OhmanMikael Oliveberg

Abstract

The ribosomal protein S6 from Thermus thermophilus has served as a model system for the study of protein folding, especially for understanding the effects of circular permutations of secondary structure elements. This study presents the structure of a permutant protein, the 96-residue P(54-55), and the structure of its 101-residue parent protein S6(wt) in solution. The data also characterizes the effects of circular permutation on the backbone dynamics of S6. Consistent with crystallographic data on S6(wt), the overall solution structures of both P(54-55) and S6(wt) show a beta-sheet of four antiparallel beta-strands with two alpha-helices packed on one side of the sheet. In clear contrast to the crystal data, however, the solution structure of S6(wt) reveals a disordered loop in the region between beta-strands 2 and 3 (Leu43-Phe60) instead of a well-ordered stretch and associated hydrophobic mini-core observed in the crystal structure. Moreover, the data for P(54-55) show that the joined wild-type N- and C-terminals form a dynamically robust stretch with a hairpin structure that complies with the in silico design. Taken together, the results explain why the loop region of the S6(wt) structure is relatively insensitive to mutat...Continue Reading

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Citations

Mar 29, 2012·Proceedings of the National Academy of Sciences of the United States of America·Martin KurnikMikael Oliveberg
Nov 26, 2011·The Journal of Biological Chemistry·Ellinor HaglundMikael Oliveberg
Jan 3, 2016·The Journal of Chemical Physics·Heiko LammertJosé N Onuchic

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