5TGW
NMR structure of apo-PS1
Summary for 5TGW
| Entry DOI | 10.2210/pdb5tgw/pdb |
| Related | 5TGY |
| NMR Information | BMRB: 30185 |
| Descriptor | PS1 (1 entity in total) |
| Functional Keywords | 4-helix bundle, coiled-coil, unknown function |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 12965.26 |
| Authors | Polizzi, N.F.,Wu, Y. (deposition date: 2016-09-28, release date: 2017-08-09, Last modification date: 2024-05-15) |
| Primary citation | Polizzi, N.F.,Wu, Y.,Lemmin, T.,Maxwell, A.M.,Zhang, S.Q.,Rawson, J.,Beratan, D.N.,Therien, M.J.,DeGrado, W.F. De novo design of a hyperstable non-natural protein-ligand complex with sub- angstrom accuracy. Nat Chem, 9:1157-1164, 2017 Cited by PubMed Abstract: Protein catalysis requires the atomic-level orchestration of side chains, substrates and cofactors, and yet the ability to design a small-molecule-binding protein entirely from first principles with a precisely predetermined structure has not been demonstrated. Here we report the design of a novel protein, PS1, that binds a highly electron-deficient non-natural porphyrin at temperatures up to 100 °C. The high-resolution structure of holo-PS1 is in sub-Å agreement with the design. The structure of apo-PS1 retains the remote core packing of the holoprotein, with a flexible binding region that is predisposed to ligand binding with the desired geometry. Our results illustrate the unification of core packing and binding-site definition as a central principle of ligand-binding protein design. PubMed: 29168496DOI: 10.1038/nchem.2846 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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