Open AccessStructure of the Drosophila melanogaster Rab6 GTPase at 1.4 Å resolution
Author(s) -
Walden Miriam,
Jenkins Huw T.,
Edwards Thomas A.
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111017453
Subject(s) - drosophila melanogaster , microbiology and biotechnology , gtpase , chemistry , biology , biochemistry , gene
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 C 2, 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 R free of 17.3%.