Cargando…
Mg(2+)-Dependent Methyl Transfer by a Knotted Protein: A Molecular Dynamics Simulation and Quantum Mechanics Study
[Image: see text] Mg(2+) is required for the catalytic activity of TrmD, a bacteria-specific methyltransferase that is made up of a protein topological knot-fold, to synthesize methylated m(1)G37-tRNA to support life. However, neither the location of Mg(2+) in the structure of TrmD nor its role in t...
Autores principales: | Perlinska, Agata P., Kalek, Marcin, Christian, Thomas, Hou, Ya-Ming, Sulkowska, Joanna I. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2020
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7462349/ https://www.ncbi.nlm.nih.gov/pubmed/32904895 http://dx.doi.org/10.1021/acscatal.0c00059 |
Ejemplares similares
-
Nucleolar Essential Protein 1 (Nep1): Elucidation of enzymatic catalysis mechanism by molecular dynamics simulation and quantum mechanics study
por: Jedrzejewski, Mateusz, et al.
Publicado: (2023) -
Restriction of S-adenosylmethionine conformational freedom by knotted protein binding sites
por: Perlinska, Agata P., et al.
Publicado: (2020) -
AlphaFold predicts novel human proteins with knots
por: Perlinska, Agata P., et al.
Publicado: (2023) -
Knot_pull—python package for biopolymer smoothing and knot detection
por: Jarmolinska, Aleksandra I, et al.
Publicado: (2019) -
In Search of Functional Advantages of Knots in Proteins
por: Dabrowski-Tumanski, Pawel, et al.
Publicado: (2016)