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

0459718 - MBÚ 2017 RIV GB eng J - Článek v odborném periodiku
Matyska Lišková, Petra - Fišer, Radovan - Macek, Pavel - Chmelík, Josef - Sýkora, Jan - Bednárová, Lucie - Konopásek, I. - Bumba, Ladislav
Probing the Ca2+-assisted pi-pi interaction during Ca2+-dependent protein folding.
Soft Matter. Roč. 12, č. 2 (2016), s. 531-541. ISSN 1744-683X. E-ISSN 1744-6848
Grant CEP: GA ČR(CZ) GAP207/11/0717; GA ČR(CZ) GBP208/12/G016; GA MŠMT LO1509
Institucionální podpora: RVO:61388971 ; RVO:61388963 ; RVO:61388955
Klíčová slova: METAL-ION-BINDING * NEISSERIA-MENINGITIDIS * RTX PROTEINS
Kód oboru RIV: CE - Biochemie; CF - Fyzikální chemie a teoretická chemie (UFCH-W)
Impakt faktor: 3.889, rok: 2016

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.
Trvalý link: http://hdl.handle.net/11104/0259921