Publication Abstract from PubMed
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 A 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 A, alpha = 90, beta = 133.12, gamma = 90 degrees . The model was refined to an R factor of 14.5% and an R(free) of 17.3%.
Structure of the Drosophila melanogaster Rab6 GTPase at 1.4 A resolution.,Walden M, Jenkins HT, Edwards TA Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Jul 1;67(Pt, 7):744-8. Epub 2011 Jun 23. PMID:21795785[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
