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Probing the Ca2 -assisted pi-pi interaction during Ca2 -dependent protein folding

Publication at Faculty of Science |
2016

Abstract

Protein folding is governed by a balance of non-covalent interactions, of which cation-pi and pi-pi play important roles. Theoretical calculations revealed a strong cooperativity between cation-pi involving alkali and alkaline earth metal ions and pi-pi interactions, but however, no experimental evidence was provided in this regard.

Here, we characterized a Ca2+-binding self-processing module (SPM), which mediates a highly-specific Ca2+-dependent autocatalytic processing of iron-regulated protein FrpC secreted by the pathogenic Gram-negative bacterium Neisseria meningitidis. The SPM undergoes a Ca2+-induced transition from an intrinsically unstructured conformation to the compact protein fold that is ultimately stabilized by the pi-pi interaction between two unique tryptophan residues arranged in the T-shaped orientation.

Moreover, the pair of tryptophans is located in a close vicinity of a calcium-binding site, suggesting the involvement of a Ca2+-assisted pi-pi interaction in the stabilization of the tertiary structure of the SPM. This makes the SPM an excellent model for the investigation of the Ca2+-assisted pi-pi interaction during Ca2+-induced protein folding.