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Publication Abstract from PubMed

Rab GTPases belong to the large family of Ras proteins. They act as key regulators of membrane organization and intracellular trafficking. Functionally, they act as switches. In the active GTP-bound form they can bind to effector proteins to facilitate the delivery of transport vesicles. Upon stimulation, the GTP is hydrolyzed and the Rab proteins undergo conformational changes in their switch regions. This study focuses on Rab2 and Rab3 from Drosophila melanogaster. Whereas Rab2 is involved in vesicle transport between the Golgi and the endoplasmatic reticulum, Rab3 is a key player in exocytosis, and in the synapse it is involved in the assembly of the presynaptic active zone. Here, high-resolution crystal structures of Rab2 and Rab3 in complex with GMPPNP and Mg(2+) are presented. In the structure of Rab3 a modified cysteine residue is observed with an enigmatic electron density attached to its thiol function.

Structures of Drosophila melanogaster Rab2 and Rab3 bound to GMPPNP.,Lardong JA, Driller JH, Depner H, Weise C, Petzoldt A, Wahl MC, Sigrist SJ, Loll B Acta Crystallogr F Struct Biol Commun. 2015 Jan 1;71(Pt 1):34-40. doi:, 10.1107/S2053230X1402617X. Epub 2015 Jan 1. PMID:25615965^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.