Crystal structure of plant aspartic proteinase prophytepsin: inactivation and vacuolar targeting.
EMBO J
; 18(14): 3947-55, 1999 Jul 15.
Article
en En
| MEDLINE
| ID: mdl-10406799
We determined at 2.3 A resolution the crystal structure of prophytepsin, a zymogen of a barley vacuolar aspartic proteinase. In addition to the classical pepsin-like bilobal main body of phytepsin, we also traced most of the propeptide, as well as an independent plant-specific domain, never before described in structural terms. The structure revealed that, in addition to the propeptide, 13 N-terminal residues of the mature phytepsin are essential for inactivation of the enzyme. Comparison of the plant-specific domain with NK-lysin indicates that these two saposin-like structures are closely related, suggesting that all saposins and saposin-like domains share a common topology. Structural analysis of prophytepsin led to the identification of a putative membrane receptor-binding site involved in Golgi-mediated transport to vacuoles.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Hordeum
/
Vacuolas
/
Catepsinas
/
Ácido Aspártico Endopeptidasas
/
Precursores Enzimáticos
Idioma:
En
Revista:
EMBO J
Año:
1999
Tipo del documento:
Article
País de afiliación:
Estados Unidos
Pais de publicación:
Reino Unido