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

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388955%3A_____%2F16%3A00459718" target="_blank" >RIV/61388955:_____/16:00459718 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61388971:_____/16:00459718 RIV/61388963:_____/16:00459718 RIV/00216208:11310/16:10318328

Výsledek na webu

<a href="http://dx.doi.org/10.1039/c5sm01796c" target="_blank" >http://dx.doi.org/10.1039/c5sm01796c</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1039/c5sm01796c" target="_blank" >10.1039/c5sm01796c</a>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

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

Popis výsledku anglicky

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.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CF - Fyzikální chemie a teoretická chemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2016

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Soft Matter

ISSN

1744-683X

e-ISSN

—

Svazek periodika

12

Číslo periodika v rámci svazku

2

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

11

Strana od-do

531-541

Kód UT WoS článku

000367259700024

EID výsledku v databázi Scopus

2-s2.0-84952310915