6I6U
Circular permutant of ribosomal protein S6, adding 9aa to N terminal of P81-82, L75A mutant
Summary for 6I6U
| Entry DOI | 10.2210/pdb6i6u/pdb |
| Descriptor | 30S ribosomal protein S6,30S ribosomal protein S6 (2 entities in total) |
| Functional Keywords | circular permutant, strand swap, local unfolding, cis-proline., ribosomal protein, designed protein |
| Biological source | Thermus thermophilus HB8 More |
| Total number of polymer chains | 2 |
| Total formula weight | 24600.09 |
| Authors | Wang, H.,Logan, D.T.,Oliveberg, M. (deposition date: 2018-11-15, release date: 2019-11-27, Last modification date: 2024-01-24) |
| Primary citation | 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 Cited by 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: 33148805DOI: 10.1073/pnas.1920455117 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.57 Å) |
Structure validation
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