Structure of Rab Escort Protein-1 in Complex with Rab Geranylgeranyltransferase
Copyright policy )Structure of Rab Escort Protein-1 in Complex with Rab Geranylgeranyltransferase
Posttranslational geranylgeranylation of Rab GTPases is catalyzed by Rab geranylgeranyltransferase (RabGGTase), which consists of a catalytic alpha/beta heterodimer and an accessory Rab escort protein (REP). The crystal structure of isoprenoid-bound RabGGTase complexed to REP-1 has been solved to 2.7 A resolution. The complex interface buries a surprisingly small surface area of ca. 680 A and is unexpectedly formed by helices 8, 10, and 12 of the RabGGTase alpha subunit and helices D and E of REP-1. We demonstrate that the affinity of RabGGTase for REP-1 is allosterically regulated by phosphoisoprenoid via a long-range trans-domain signal transduction event. Comparing the structure of REP-1 with the closely related RabGDI, we conclude that the specificity of the REP:RabGGTase interaction is defined by differently positioned phenylalanine residues conserved in the REP and GDI subfamilies.
- University of Queensland Australia
- University of Queensland Australia
- Sorbonne University France
- Queensland University of Technology Australia
- Lomonosov Moscow State University Russian Federation
System, Models, Molecular, Macromolecular Substances, Protein Conformation, Molecular Sequence Data, Expression, In Vitro Techniques, 0601 Biochemistry and Cell Biology, Gdp, Association, Animals, Amino Acid Sequence, Molecular Biology, Guanine Nucleotide Dissociation Inhibitors, Prenylation, Alkyl and Aryl Transferases, Binding Sites, Sequence Homology, Amino Acid, 500, Cell Biology, Binding, 06 Biological Sciences, Lipid Metabolism, Nucleotide dissociation inhibitor, rab3A GTP-Binding Protein, [SDV] Life Sciences [q-bio], Mutagenesis, rab GTP-Binding Proteins, Mechanism, Transferase, Substrate, 03 Chemical Sciences, Signal Transduction
System, Models, Molecular, Macromolecular Substances, Protein Conformation, Molecular Sequence Data, Expression, In Vitro Techniques, 0601 Biochemistry and Cell Biology, Gdp, Association, Animals, Amino Acid Sequence, Molecular Biology, Guanine Nucleotide Dissociation Inhibitors, Prenylation, Alkyl and Aryl Transferases, Binding Sites, Sequence Homology, Amino Acid, 500, Cell Biology, Binding, 06 Biological Sciences, Lipid Metabolism, Nucleotide dissociation inhibitor, rab3A GTP-Binding Protein, [SDV] Life Sciences [q-bio], Mutagenesis, rab GTP-Binding Proteins, Mechanism, Transferase, Substrate, 03 Chemical Sciences, Signal Transduction
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