title: Structure of the Drosophila melanogaster Rab6 GTPase at 1.4 Å resolution.
abstract: Rab6 is a small GTPase that belongs to the p21 Ras superfamily. It is involved in vesicle trafficking between the Golgi apparatus and endosomes/ER in eukaryotes. The GDP-bound inactive protein undergoes conformational changes when the nucleotide is exchanged to GTP, allowing Rab6 to interact with a variety of different effector proteins. To further understand how these changes affect downstream protein binding, the crystal structure of Rab6 from Drosophila melanogaster has been solved to 1.4 Å resolution, the highest resolution for a Rab6 structure to date. The crystals belonged to space group C2, with unit-cell parameters a=116.5, b=42.71, c=86.86 Å, α=90, β=133.12, γ=90°. The model was refined to an R factor of 14.5% and an Rfree of 17.3%.
authors.affiliation: Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, England.
authors.forename: Miriam
authors.initials: M
authors.lastname: Walden
authors.forename: Huw T
authors.initials: HT
authors.lastname: Jenkins
authors.forename: Thomas A
authors.initials: TA
authors.lastname: Edwards
mesh_terms: D000818:Animals; D018360:Crystallography, X-Ray; D004331:Drosophila melanogaster / Q000201:enzymology*; D006160:Guanosine Triphosphate / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D013379:Substrate Specificity; D020691:rab GTP-Binding Proteins / Q000737:chemistry* / Q000378:metabolism
chemical_list: C094135:Rab6 protein; D006160:Guanosine Triphosphate; D020691:rab GTP-Binding Proteins