Pregled bibliografske jedinice broj: 1180224
Computational study of the mycobacterium tuberculosis transcriptional repressor MntR
Computational study of the mycobacterium tuberculosis transcriptional repressor MntR // 27th Croatian Meeting of Chemists and Chemical Engineers and 5th Symposium Vladimir Prelog : Book of Abstracts / Marković, Dean ; Meštrović, Ernest ; Namjesnik, Danijel ; Tomašić, Vesna (ur.).
Zagreb: Hrvatsko kemijsko društvo, 2021. str. 272-272 (poster, domaća recenzija, sažetak, znanstveni)
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Naslov
Computational study of the mycobacterium
tuberculosis transcriptional repressor MntR
Autori
Jelić Matošević, Zoe ; Brajković, Mislav ; Neves, Rui P P ; Fernandes, Pedro Alexandrino ; Bertoša, Branimir
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni
Izvornik
27th Croatian Meeting of Chemists and Chemical Engineers and 5th Symposium Vladimir Prelog : Book of Abstracts
/ Marković, Dean ; Meštrović, Ernest ; Namjesnik, Danijel ; Tomašić, Vesna - Zagreb : Hrvatsko kemijsko društvo, 2021, 272-272
Skup
27. hrvatski skup kemičara i kemijskih inženjera (27HSKIKI)
Mjesto i datum
Veli Lošinj, Hrvatska, 05.10.2021. - 08.10.2021
Vrsta sudjelovanja
Poster
Vrsta recenzije
Domaća recenzija
Ključne riječi
molekulska dinamika, transkripcijski faktori, MntR
(molecular dynamics, transcription factors, MntR)
Sažetak
Manganese homeostasis in Mycobacterium tuberculosis, the causative agent of tuberculosis, is regulated by the transcriptional repressor MntR from the IdeR family of transcriptional regulators. Tuberculosis is an important health concern in the world today, which is exacerbated by the advent of multi-drug resistant strains.[1] MntR is allosterically activated for DNA-binding by manganese. It harbors two manganese binding sites, of which one is a binuclear site accommodating two manganese ions. MntR is composed of three domains - the N-terminal DNA-binding domain, the central dimerization domain and the C- terminal FeoA domain and it binds to DNA as a dimer.[1] The FeoA domain is present in many members of the IdeR family. However, its function has only recently been partially explained for the protein MtsR.[2] To start our investigation of M. tuberculosis MntR, we parametrized the interaction of protein and manganese ions using a bonded model approach. First, we optimized the binding site geometry using DFT calculations at the B3LYP/SDD:6-31G(d, p) level of theory. We then developed force field parameters using the approach by Li.[3] Finally, we used molecular dynamics simulation to study the dynamic behavior of MntR both in its apo and manganesebound forms.
Izvorni jezik
Engleski
Znanstvena područja
Kemija, Biologija
POVEZANOST RADA
Projekti:
HRZZ-IP-2020-02-3446 - Manganovi metalosenzori (MaMes) (Bertoša, Branimir, HRZZ - 2020-02) ( CroRIS)
HRZZ-IP-2020-02-3446 - Manganovi metalosenzori (MaMes) (Bertoša, Branimir, HRZZ - 2020-02) ( CroRIS)
Ustanove:
Prirodoslovno-matematički fakultet, Zagreb