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Purification, crystallization and X-ray crystallographic analysis of human RAB11(S20V), a constitutively active GTP-binding form.


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 293?K. X-ray diffraction data were collected to a resolution of 2.4?Å from a crystal belonging to space group I4, with unit-cell parameters a = 74.11, b = 74.11, c = 149.44?Å. The asymmetric unit was estimated to contain two molecules of RAB11(S20V).

SUBMITTER: Kim CM 

PROVIDER: S-EPMC4601587 | BioStudies | 2015-01-01

REPOSITORIES: biostudies

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