Nucleation of an Activating Conformational Change by a Cation-π Interaction.
Biochemistry
; 58(32): 3408-3412, 2019 08 13.
Article
em En
| MEDLINE
| ID: mdl-31339702
ABSTRACT
As a key molecule in biology, adenosine triphosphate (ATP) has numerous crucial functions in, for instance, energetics, post-translational modifications, nucleotide biosynthesis, and cofactor metabolism. Here, we have discovered an intricate interplay between the enzyme adenylate kinase and its substrate ATP. The side chain of an arginine residue was found to be an efficient sensor of the aromatic moiety of ATP through the formation of a strong cation-π interaction. In addition to recognition, the interaction was found to have dual functionality. First, it nucleates the activating conformational transition of the ATP binding domain and also affects the specificity in the distant AMP binding domain. In light of the functional consequences resulting from the cation-π interaction, it is possible that the mode of ATP recognition may be a useful tool in enzyme design.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Trifosfato de Adenosina
/
Adenilato Quinase
Idioma:
En
Revista:
Biochemistry
Ano de publicação:
2019
Tipo de documento:
Article