6I6S

Circular permutant of ribosomal protein S6, adding 9aa to C terminal of P68-69, L75A mutant

6I6S の概要

• エントリーDOI: 10.2210/pdb6i6s/pdb
• 分子名称: 30S ribosomal protein S6,30S ribosomal protein S6,30S ribosomal protein S6,30S ribosomal protein S6,30S ribosomal protein S6,30S ribosomal protein S6,30S ribosomal protein S6,30S ribosomal protein S6, POTASSIUM ION, SODIUM ION, ... (4 entities in total)
• 機能のキーワード: circular permutant, strand swap, local unfolding, cis-proline., ribosomal protein, designed protein
• 由来する生物種: Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 24637.99

構造登録者

Wang, H.,Logan, D.T.,Oliveberg, M. (登録日: 2018-11-15, 公開日: 2019-11-27, 最終更新日: 2024-01-24)

主引用文献

Wang, H.,Logan, D.T.,Danielsson, J.,Oliveberg, M.
Exposing the distinctive modular behavior of beta-strands and alpha-helices in folded proteins.
Proc.Natl.Acad.Sci.USA, 117:28775-28783, 2020

PubMed Abstract: Although folded proteins are commonly depicted as simplistic combinations of β-strands and α-helices, the actual properties and functions of these secondary-structure elements in their native contexts are just partly understood. The principal reason is that the behavior of individual β- and α-elements is obscured by the global folding cooperativity. In this study, we have circumvented this problem by designing frustrated variants of the mixed α/β-protein S6, which allow the structural behavior of individual β-strands and α-helices to be targeted selectively by stopped-flow kinetics, X-ray crystallography, and solution-state NMR. Essentially, our approach is based on provoking intramolecular "domain swap." The results show that the α- and β-elements have quite different characteristics: The swaps of β-strands proceed via global unfolding, whereas the α-helices are free to swap locally in the native basin. Moreover, the α-helices tend to hybridize and to promote protein association by gliding over to neighboring molecules. This difference in structural behavior follows directly from hydrogen-bonding restrictions and suggests that the protein secondary structure defines not only tertiary geometry, but also maintains control in function and structural evolution. Finally, our alternative approach to protein folding and native-state dynamics presents a generally applicable strategy for in silico design of protein models that are computationally testable in the microsecond-millisecond regime.

PubMed: 33148805
DOI: 10.1073/pnas.1920455117

実験手法

X-RAY DIFFRACTION (1.46 Å)