Crystallization and preliminary X-ray crystallographic studies of Rab6A '(Q72L): a GTP-locked form

Title
Crystallization and preliminary X-ray crystallographic studies of Rab6A '(Q72L): a GTP-locked form
Author(s)
박현호장태호[장태호]신영철[신영철]윤종환[윤종환]전주홍[전주홍]
Keywords
TRANS-GOLGI NETWORK; PROTEIN; RAB6A; BINDING; GTPASES; MEMBER
Issue Date
201209
Publisher
WILEY-BLACKWELL
Citation
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS, v.68, pp.1077 - 1080
Abstract
Rab6A, a member of the Ras superfamily of small G proteins, is involved in the regulation of vesicle trafficking, which is critical for endocytosis, cell differentiation and cell growth. Rab6A can exist in two isoforms termed Rab6A and Rab6A'. The substitution of Gln72 by Leu (Q72L) in the Rab6A family blocks GTP-hydrolysis activity, and this mutation usually causes the Rab6A protein to be in a constitutively active form. In this study, in order to understand the functional uniqueness of Rab6A' and the molecular mechanism of the control of activity by GTP and GDP from the crystal structure, a Rab6A'(Q72L) mutant form was overexpressed in Escherichia coli with an engineered N-terminal His tag. Rab6A'(Q72L) was then purified to homogeneity and crystallized at 293 K. X-ray diffraction data were collected to a resolution of 1.9 angstrom from a crystal belonging to space group P22121 with unit-cell parameters a= 36.84, b = 96.78, c=109.99 angstrom. The asymmetric unit was estimated to contain two molecules.
URI
http://hdl.handle.net/YU.REPOSITORY/27302http://dx.doi.org/10.1107/S1744309112030874
ISSN
1744-3091
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이과대학 > 화학생화학부 > Articles
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