Allosteric mechanism of MntR transcription factor from alkalophilic bacterium Halalkalibacterium halodurans.
J Biomol Struct Dyn
; : 1-15, 2024 Feb 12.
Article
em En
| MEDLINE
| ID: mdl-38345054
ABSTRACT
Bacterium Halalkalibacterium halodurans is an industrially important alkalophilic bacteria. It is recognized as a producer of enzymes such as ß-galactosidase, xylanase, amylase and protease which are able to function at higher pH values and thus can be used in textile, food, paper industry and more. This bacterium, as any other bacterium, requires a sensitive mechanism for regulation of homeostasis of manganese ions (Mn2+) in order to survive. The key protein regulating this mechanism in H. halodurans is MntR - a transcriptional factor that binds to DNA and regulates the transcription of genes for proteins involved in manganese homeostasis. Long range all-atom molecular dynamics (MD) simulations, from 500 ns up to 1.25 µs, were used to study different forms of H. halodurans MntR in order to investigate the differences in the protein's structural and dynamical properties upon Mn2+ binding. Simulations revealed an allosteric mechanism which is activated by Mn2+ binding. The results of simulations show that Mn2+ binding alters the non-covalent interaction network of the protein structure which leads to a conformational change that primarily affects the positions of the DNA binding domains and, consequently, the DNA binding affinity of H. halodurans MntR. The key amino acid residues of the proposed mechanism were identified and their role in the proposed mechanism was computationally confirmed by MD simulations of in silico mutants.Communicated by Ramaswamy H. Sarma.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Tipo de estudo:
Prognostic_studies
Idioma:
En
Revista:
J Biomol Struct Dyn
Ano de publicação:
2024
Tipo de documento:
Article
País de afiliação:
Croácia