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

Result code in 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>
Alternative codes found
RIV/61388971:_____/16:00459718 RIV/61388963:_____/16:00459718 RIV/00216208:11310/16:10318328
Result on the web
<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>

Result language
angličtina
Original language name
Probing the Ca2+-assisted pi-pi interaction during Ca2+-dependent protein folding
Original language description
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.
Czech name
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Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CF - Physical chemistry and theoretical chemistry
OECD FORD branch
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Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year
2016
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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