The activation cycle of Rab GTPase Ypt32 reveals structural determinants of effector recruitment and GDI binding
Copyright policy )The activation cycle of Rab GTPase Ypt32 reveals structural determinants of effector recruitment and GDI binding
Rab GTPases localize to distinct sub-cellular compartments and regulate vesicle trafficking in eukaryotic cells. Yeast Rabs Ypt31/32 and Sec4 have 68% homology and bind to common interactors, yet play distinct roles in the transport of exocytic vesicles. The structures of Ypt31/32 have not previously been reported in the uncomplexed state. We describe the crystal structures of GTP and GDP forms of Ypt32 to understand the molecular basis for Rab function. The structure of Ypt32(GTP) reveals that the switch II conformation is distinct from Sec4(GTP) in spite of a highly conserved amino acid sequence. Also, Ypt32(GDP) reveals a remarkable change in conformation of the switch II helix induced by binding to GDI, which has not been described previously.
- University of Michigan–Ann Arbor United States
- Life Sciences Institute United States
- Trinity College Dublin Ireland
- UNIVERSITY OF MICHIGAN
- University of Michigan–Flint United States
Myosin 2p, RabSF, Saccharomyces cerevisiae Proteins, Rab-binding domain, Protein Conformation, Science, Molecular Sequence Data, Vesicle trafficking, Crystallography, X-Ray, Guanosine Diphosphate, RBD, Sec4, Amino Acid Sequence, Myo2p, Ypt32, Conserved Sequence, X-ray crystallography, Guanine Nucleotide Dissociation Inhibitors, Binding Sites, Rab sub-family specific regions, Effectors, Biological Chemistry, rab GTP-Binding Proteins, Guanosine Triphosphate, Sequence Alignment, Rab GTPase
Myosin 2p, RabSF, Saccharomyces cerevisiae Proteins, Rab-binding domain, Protein Conformation, Science, Molecular Sequence Data, Vesicle trafficking, Crystallography, X-Ray, Guanosine Diphosphate, RBD, Sec4, Amino Acid Sequence, Myo2p, Ypt32, Conserved Sequence, X-ray crystallography, Guanine Nucleotide Dissociation Inhibitors, Binding Sites, Rab sub-family specific regions, Effectors, Biological Chemistry, rab GTP-Binding Proteins, Guanosine Triphosphate, Sequence Alignment, Rab GTPase
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