title: Structures of Drosophila melanogaster Rab2 and Rab3 bound to GMPPNP.
abstract: 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 Mg2+ are presented. In the structure of Rab3 a modified cysteine residue is observed with an enigmatic electron density attached to its thiol function.
authors.affiliation: Institut für Chemie und Biochemie Abteilung Strukturbiochemie, Freie Universität Berlin, Takustrasse 6, 15195 Berlin, Germany.
authors.forename: Jennifer A
authors.initials: JA
authors.lastname: Lardong
authors.affiliation: Institut für Chemie und Biochemie Abteilung Strukturbiochemie, Freie Universität Berlin, Takustrasse 6, 15195 Berlin, Germany.
authors.forename: Jan H
authors.initials: JH
authors.lastname: Driller
authors.affiliation: Biologie Abteilung Genetik, Freie Universität Berlin, Takustrasse 6, 15195 Berlin, Germany.
authors.forename: Harald
authors.initials: H
authors.lastname: Depner
authors.affiliation: Institut für Chemie und Biochemie, BioSupraMol Core Facility, Freie Universität Berlin, Thielallee 63, 15195 Berlin, Germany.
authors.forename: Christoph
authors.initials: C
authors.lastname: Weise
authors.affiliation: Biologie Abteilung Genetik, Freie Universität Berlin, Takustrasse 6, 15195 Berlin, Germany.
authors.forename: Astrid
authors.initials: A
authors.lastname: Petzoldt
authors.affiliation: Institut für Chemie und Biochemie Abteilung Strukturbiochemie, Freie Universität Berlin, Takustrasse 6, 15195 Berlin, Germany.
authors.forename: Markus C
authors.initials: MC
authors.lastname: Wahl
authors.affiliation: Biologie Abteilung Genetik, Freie Universität Berlin, Takustrasse 6, 15195 Berlin, Germany.
authors.forename: Stephan J
authors.initials: SJ
authors.lastname: Sigrist
authors.affiliation: Institut für Chemie und Biochemie Abteilung Strukturbiochemie, Freie Universität Berlin, Takustrasse 6, 15195 Berlin, Germany.
authors.forename: Bernhard
authors.initials: B
authors.lastname: Loll
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D029721:Drosophila Proteins / Q000737:chemistry*; D004331:Drosophila melanogaster / Q000201:enzymology*; D006165:Guanylyl Imidodiphosphate / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding; D017433:Protein Structure, Secondary; D040681:Structural Homology, Protein; D020693:rab2 GTP-Binding Protein / Q000737:chemistry*; D020692:rab3 GTP-Binding Proteins / Q000737:chemistry*
chemical_list: D029721:Drosophila Proteins; D006165:Guanylyl Imidodiphosphate; D020693:rab2 GTP-Binding Protein; D020692:rab3 GTP-Binding Proteins
keywords: GMPPNP; GTPase; Rab; cysteine modification