Parametrization of the Mn2+ Binding Site of Protein SloR (S. mutans) Starting from the Zn2+ bound Crystal Structure (CROSBI ID 731357)
Prilog sa skupa u zborniku | sažetak izlaganja sa skupa | domaća recenzija
Podaci o odgovornosti
Radman, K. ; Jelić Matošević, Z. ; Neves, R. P. P. ; Fernandes, P. A. ; Bertoša, B
engleski
Parametrization of the Mn2+ Binding Site of Protein SloR (S. mutans) Starting from the Zn2+ bound Crystal Structure
The primary causative agent of human dental caries is Streptococcus mutans, an oral pathogen that grows as a plaque biofilm on the tooth surface. Metal ion homeostasis is essential for the growth and survival of most microorganisms, including the bacteria S. mutans.1 Divalent metal ions, such as Fe2+ and Mn2+, are important enzyme cofactors and stabilizing components of proteins in various key metabolic pathways. The metaloregulatory protein SloR has an important role in maintaining homeostasis of Mn2+ ions in S. mutans. As a transcriptional factor, SloR regulates metal ion transport upon binding to DNA in response to manganese availability.2 In order to investigate the structural and dynamical properties of the protein and their changes upon Mn2+ binding to SloR. Adequate parametrization of interaction between Mn2+ ions and protein is necessary fro such study. The parametrisas using a bonded model scheme that was presented by Pengfei and Merz3 was used.
Transcription factors, manganese, parametrization
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Podaci o prilogu
44-44.
2022.
objavljeno
Podaci o matičnoj publikaciji
Supramolecular Chemistry 2022: Book of Abstracts
Frkanec, Leo ; Namjesnik, Danijel ; Tomišić, Vladislav
Zagreb: Institut Ruđer Bošković
Podaci o skupu
5. simpozij supramolekulske kemije
poster
08.12.2022-08.12.2022
Zagreb, Hrvatska