Purification, crystallization and X-ray crystallographic analysis of human RAB11(S20V), a constitutively active GTP-binding form.
Acta Crystallogr F Struct Biol Commun
; 71(Pt 10): 1247-50, 2015 Oct.
Article
em En
| MEDLINE
| ID: mdl-26457514
ABSTRACT
RAB11, a member of the Ras superfamily of small G proteins, is involved in the regulation of vesicle trafficking during endosome recycling. Substitution of Ser20 by Val20 in Rab11 [RAB11(S20V)] inhibits its GTP hydrolysis activity and produces a constitutively active GTP-binding form. In this study, the RAB11(S20V) mutant was overexpressed in Escherichia coli with an engineered C-terminal His tag. RAB11(S20V) was then purified to homogeneity and was crystallized at 293â
K. X-ray diffraction data were collected to a resolution of 2.4â
Å from a crystal belonging to space group I4, with unit-cell parameters a = 74.11, b = 74.11, c = 149.44â
Å. The asymmetric unit was estimated to contain two molecules of RAB11(S20V).
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas rab de Ligação ao GTP
/
Guanosina Trifosfato
Limite:
Humans
Idioma:
En
Revista:
Acta Crystallogr F Struct Biol Commun
Ano de publicação:
2015
Tipo de documento:
Article