3JZA

Crystal structure of human Rab1b in complex with the GEF domain of DrrA/SidM from Legionella pneumophila

Summary for 3JZA

• Entry DOI: 10.2210/pdb3jza/pdb
• Related: 3JZ9
• Descriptor: Ras-related protein Rab-1B, Uncharacterized protein DrrA, PHOSPHATE ION, ... (4 entities in total)
• Functional Keywords: rabgdi, rabgef, gdi, gef, gdf, gdi displacement factor, gtp-binding, lipoprotein, membrane, nucleotide-binding, prenylation, protein transport, transport protein
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm : Q9H0U4; Secreted : Q5ZSQ3
• Total number of polymer chains: 2
• Total formula weight: 41860.48

Authors

Schoebel, S.,Oesterlin, L.K.,Blankenfeldt, W.,Goody, R.S.,Itzen, A. (deposition date: 2009-09-23, release date: 2010-01-19, Last modification date: 2024-02-21)

Primary citation

Schoebel, S.,Oesterlin, L.K.,Blankenfeldt, W.,Goody, R.S.,Itzen, A.
RabGDI displacement by DrrA from Legionella is a consequence of its guanine nucleotide exchange activity.
Mol.Cell, 36:1060-1072, 2009

PubMed Abstract: Prenylated Rab proteins exist in the cytosol as soluble, high-affinity complexes with GDI that need to be disrupted for membrane attachment and targeting of Rab proteins. The Legionella pneumophila protein DrrA displaces GDI from Rab1:GDI complexes, incorporating Rab1 into Legionella-containing vacuoles and activating Rab1 by exchanging GDP for GTP. Here, we present the crystal structure of a complex between the GEF domain of DrrA and Rab1 and a detailed kinetic analysis of this exchange. DrrA efficiently catalyzes nucleotide exchange and mimics the general nucleotide exchange mechanism of mammalian GEFs for Ras-like GTPases. We show that the GEF activity of DrrA is sufficient to displace prenylated Rab1 from the Rab1:GDI complex. Thus, apparent GDI displacement by DrrA is linked directly to nucleotide exchange, suggesting a basic model for GDI displacement and specificity of Rab localization that does not require discrete GDI displacement activity.

PubMed: 20064470
DOI: 10.1016/j.molcel.2009.11.014

Experimental method

X-RAY DIFFRACTION (1.8 Å)