Crystal structure of nucleotide-free dynamin.
Nature
; 477(7366): 556-60, 2011 Sep 18.
Article
en En
| MEDLINE
| ID: mdl-21927000
ABSTRACT
Dynamin is a mechanochemical GTPase that oligomerizes around the neck of clathrin-coated pits and catalyses vesicle scission in a GTP-hydrolysis-dependent manner. The molecular details of oligomerization and the mechanism of the mechanochemical coupling are currently unknown. Here we present the crystal structure of human dynamin 1 in the nucleotide-free state with a four-domain architecture comprising the GTPase domain, the bundle signalling element, the stalk and the pleckstrin homology domain. Dynamin 1 oligomerized in the crystals via the stalks, which assemble in a criss-cross fashion. The stalks further interact via conserved surfaces with the pleckstrin homology domain and the bundle signalling element of the neighbouring dynamin molecule. This intricate domain interaction rationalizes a number of disease-related mutations in dynamin 2 and suggests a structural model for the mechanochemical coupling that reconciles previous models of dynamin function.
Texto completo:
1
Bases de datos:
MEDLINE
Asunto principal:
Dinamina I
/
Nucleótidos
Límite:
Humans
Idioma:
En
Revista:
Nature
Año:
2011
Tipo del documento:
Article
País de afiliación:
Alemania