5TGY

NMR structure of holo-PS1

Summary for 5TGY

• Entry DOI: 10.2210/pdb5tgy/pdb
• Related: 5TGW
• NMR Information: BMRB: 30186
• Descriptor: PS1, [5,10,15,20-tetrakis(trifluoromethyl)porphyrinato(2-)-kappa~4~N~21~,N~22~,N~23~,N~24~]zinc (2 entities in total)
• Functional Keywords: 4-helix bundle, coiled-coil, holoprotein, unknown function
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 13611.00

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

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: 29168496
DOI: 10.1038/nchem.2846

Experimental method

SOLUTION NMR