Systematic elucidation of the second coordination sphere effect on the structure and properties of a blue copper protein, pseudoazurin.
J Inorg Biochem
; 246: 112292, 2023 09.
Article
en En
| MEDLINE
| ID: mdl-37354604
ABSTRACT
The rational structural and computational studies of a blue copper protein, pseudoazurin (PAz), and its Met16X (X = Phe, Leu, Val, Ile) variants gave clear functional meanings of the noncovalent interaction (NCI) through the second coordination sphere. The high-resolution X-ray crystal structures of Met16X PAz demonstrated that the active site geometry is significantly affected by the substitution of Met16, which is located within the NCI distance from the His81 imidazole ring at the copper active site. The computational chemistry calculations based on the crystal structure analyses confirmed that the NCI of S-π/CH-π (wild-type), π-π (Met16Phe), double CH-π (Met16Leu), and single CH-π (Met16Val and Met16Ile). The estimated interaction energies for the NCI demonstrated that the fine-tuning of the protein stability and Cu site properties form the second coordination sphere of PAz.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Azurina
/
Cobre
Idioma:
En
Revista:
J Inorg Biochem
Año:
2023
Tipo del documento:
Article
País de afiliación:
Japón