2y8e
Crystal structure of D. melanogaster Rab6 GTPase bound to GMPPNP
Structural highlights
FunctionRAB6_DROME Protein transport. Regulator of membrane traffic from the Golgi apparatus towards the endoplasmic reticulum (ER). Mediates membrane trafficking during egg chamber growth and organization, possibly upstream of exocyst component sec5. Also during oogenesis, plays a role, together with BicD but independently of sec5, in the polarization of the oocyte microtubule cytoskeleton, in the localization of oskar mRNA and in the anterodorsal secretion of grk. Required for anterograde opsin transport through the ER-Golgi complex. Plays a role, together with Rich, in regulating CadN transport in photoreceptor cells which is required for the formation of normal synaptic connections between axons from the inner photoreceptor cells in the eye and postsynaptic cells in the brain medulla layer M6. Necessary for proper development of bristle shafts of macrochaete and microchaete on the head, thorax and scutellum. Modulates Notch signaling. As a key regulator of vesicular traffic, plays a critical role in the regulation of actin organization and is required for normal rates of phagocytic uptake during phagocytosis involved in defense against viral and fungal infection.[1] [2] [3] [4] [5] [6] [7] Publication Abstract from PubMedRab6 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[8] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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