title: Crystallization and preliminary X-ray crystallographic studies of Rab6A'(Q72L): a GTP-locked form.
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 Å from a crystal belonging to space group P22(1)2(1) with unit-cell parameters a = 36.84, b = 96.78, c = 109.99 Å. The asymmetric unit was estimated to contain two molecules.
authors.affiliation: Department of Physiology, Seoul National University College of Medicine, Seoul 110-799, Republic of Korea.
authors.forename: Young-Cheul
authors.initials: YC
authors.lastname: Shin
authors.forename: Tae-Ho
authors.initials: TH
authors.lastname: Jang
authors.forename: Jong Hwan
authors.initials: JH
authors.lastname: Yoon
authors.forename: Ju-Hong
authors.initials: JH
authors.lastname: Jeon
authors.forename: Hyun Ho
authors.initials: HH
authors.lastname: Park
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D006160:Guanosine Triphosphate / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D020691:rab GTP-Binding Proteins / Q000737:chemistry* / Q000378:metabolism
chemical_list: D006160:Guanosine Triphosphate; C417211:RAB6C protein, human; D020691:rab GTP-Binding Proteins