5UBS
Solution NMR Structure of NERD-S, a natively folded pentamutant of the B1 domain of streptococcal protein G (GB1) with a solvent-exposed Trp43
Summary for 5UBS
| Entry DOI | 10.2210/pdb5ubs/pdb |
| Related | 5UB0 5UCE 5UCF |
| NMR Information | BMRB: 30221 |
| Descriptor | Immunoglobulin G-binding protein G (1 entity in total) |
| Functional Keywords | dynamics, computational design, conformational exchange, immunoglobulin-binding, de novo protein |
| Biological source | Streptococcus sp. GX7805 |
| Total number of polymer chains | 1 |
| Total formula weight | 6289.93 |
| Authors | Damry, A.M.,Davey, J.A.,Goto, N.K.,Chica, R.A. (deposition date: 2016-12-21, release date: 2017-08-23, Last modification date: 2024-05-15) |
| Primary citation | Davey, J.A.,Damry, A.M.,Goto, N.K.,Chica, R.A. Rational design of proteins that exchange on functional timescales. Nat. Chem. Biol., 13:1280-1285, 2017 Cited by PubMed Abstract: Proteins are intrinsically dynamic molecules that can exchange between multiple conformational states, enabling them to carry out complex molecular processes with extreme precision and efficiency. Attempts to design novel proteins with tailored functions have mostly failed to yield efficiencies matching those found in nature because standard methods do not allow the design of exchange between necessary conformational states on a functionally relevant timescale. Here we developed a broadly applicable computational method to engineer protein dynamics that we term meta-multistate design. We used this methodology to design spontaneous exchange between two novel conformations introduced into the global fold of Streptococcal protein G domain β1. The designed proteins, named DANCERs, for dynamic and native conformational exchangers, are stably folded and switch between predicted conformational states on the millisecond timescale. The successful introduction of defined dynamics on functional timescales opens the door to new applications requiring a protein to spontaneously access multiple conformational states. PubMed: 29058725DOI: 10.1038/nchembio.2503 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
