Structural basis for sugar translocation through maltoporin channels at 3.1 A resolution.
Science
; 267(5197): 512-4, 1995 Jan 27.
Article
en En
| MEDLINE
| ID: mdl-7824948
ABSTRACT
Trimeric maltoporin (LamB protein) facilitates the diffusion of maltodextrins across the outer membrane of Gram-negative bacteria. The crystal structure of maltoporin from Escherichia coli, determined to a resolution of 3.1 angstroms, reveals an 18-stranded, antiparallel beta-barrel that forms the framework of the channel. Three inwardly folded loops contribute to a constriction about halfway through the channel. Six contingent aromatic residues line the channel and form a path from the vestibule to the periplasmic outlet. Soaking of a crystal with maltotriose revealed binding of the sugar to this hydrophobic track across the constriction, which suggests that maltose and linear oligosaccharides may be translocated across the membrane by guided diffusion along this path.
Buscar en Google
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Oligosacáridos
/
Receptores Virales
/
Membrana Celular
/
Porinas
/
Escherichia coli
/
Maltosa
Tipo de estudio:
Prognostic_studies
Idioma:
En
Revista:
Science
Año:
1995
Tipo del documento:
Article
País de afiliación:
Suiza