Dynamic study of small toxic hydrophobic proteins PepA1 and PepG1 of Staphylococcus aureus
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F22%3A00562204" target="_blank" >RIV/61388971:_____/22:00562204 - isvavai.cz</a>
Alternative codes found
RIV/86652036:_____/22:00562204 RIV/00216208:11110/22:10450210 RIV/00216208:11310/22:10450210
Result on the web
<a href="https://www.sciencedirect.com/science/article/pii/S0141813022016245?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0141813022016245?via%3Dihub</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.ijbiomac.2022.07.192" target="_blank" >10.1016/j.ijbiomac.2022.07.192</a>
Alternative languages
Result language
angličtina
Original language name
Dynamic study of small toxic hydrophobic proteins PepA1 and PepG1 of Staphylococcus aureus
Original language description
Toxin-antitoxin (TA) systems are small genetic elements which encode toxin proteins that interfere with vital cellular functions. PepA1 and PepG1 toxin proteins, known also as SprA1 and SprG1, are type I TA. In Staphylococcus aureus (S. aureus), their expression without the antitoxin counterparts (SprA1AS and SprF1), is lethal to the pathogen. Molecular Dynamics (MD) simulation was performed for PepA1 and PepG1 to understand their dynamic state, conformational changes, and their toxicity. The protein structures were constructed and used for MD simulation and the conformational changes, stability, flexibility, fluctuations, hydrophobicity, and role of their dynamic state on function prediction were studied extensively by GROMACS MD simulation analysis tools. In silico study indicated that the PepA1 and PepG1 proteins change their structural conformation from an open to closed state where PepA1 conformational changes were faster (10 ns) than PepG1 (20 ns) while PepG1 exerted more stability and flexibility than PepA1. According to SASA values, PepG1 is more hydrophobic than the PepA1 and forms fewer hydrogen bonds than PepA1. The in vivo study with PepA1 and PepG1 proteins provided evidence that both the conformation changes between the open and closed states and the amino acid sequence are crucial for peptide toxicity.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10404 - Polymer science
Result continuities
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
Others
Publication year
2022
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
International Journal of Biological Macromolecules
ISSN
0141-8130
e-ISSN
1879-0003
Volume of the periodical
219
Issue of the periodical within the volume
OCT 31 2022
Country of publishing house
GB - UNITED KINGDOM
Number of pages
12
Pages from-to
1360-1371
UT code for WoS article
000861506400005
EID of the result in the Scopus database
2-s2.0-85138063621