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Dynamic study of small toxic hydrophobic proteins PepA1 and PepG1 of Staphylococcus aureus
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SYSNO ASEP 0562204 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Dynamic study of small toxic hydrophobic proteins PepA1 and PepG1 of Staphylococcus aureus Author(s) Sur, Vishma Pratap (BTO-N)
Šimoník, Ondřej (BTO-N)
Novotná, Michaela (MBU-M)
Mazumdar, Aninda (MBU-M)
Liška, F. (CZ)
Vimberg, Vladimír (MBU-M) ORCID
Komrsková, Kateřina (BTO-N) ORCIDNumber of authors 7 Source Title International Journal of Biological Macromolecules. - : Elsevier - ISSN 0141-8130
Roč. 219, OCT 31 2022 (2022), s. 1360-1371Number of pages 12 s. Language eng - English Country GB - United Kingdom Keywords Toxinantitoxin system ; Staphylococcus aureus ; PepA1 ; PepG1 ; Molecular dynamics simulation ; Cloning Subject RIV CD - Macromolecular Chemistry OECD category Polymer science R&D Projects NU20-03-00309 GA MZd - Ministry of Health (MZ) ED1.1.00/02.0109 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) Method of publishing Limited access Institutional support BTO-N - RVO:86652036 ; MBU-M - RVO:61388971 UT WOS 000861506400005 EID SCOPUS 85138063621 DOI 10.1016/j.ijbiomac.2022.07.192 Annotation 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. Workplace Institute of Biotechnology Contact Monika Kopřivová, Monika.Koprivova@ibt.cas.cz, Tel.: 325 873 700 Year of Publishing 2023 Electronic address https://www.sciencedirect.com/science/article/pii/S0141813022016245?via%3Dihub
Number of the records: 1