2WWX

Crystal structure of the SidM/DrrA(GEF/GDF domain)-Rab1(GTPase domain) complex

Summary for 2WWX

• Entry DOI: 10.2210/pdb2wwx/pdb
• Related: 2FOL
• Descriptor: RAS-RELATED PROTEIN RAB-1, DRRA (3 entities in total)
• Functional Keywords: golgi apparatus, protein transport, er-golgi transport, endoplasmic reticulum, prenylation, lipoprotein, nucleotide-binding
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Golgi apparatus: P62820; Secreted: Q29ST3
• Total number of polymer chains: 2
• Total formula weight: 44169.41

Authors

Suh, H.Y.,Lee, D.W.,Woo, J.S.,Oh, B.H. (deposition date: 2009-10-30, release date: 2009-12-08, Last modification date: 2015-04-01)

Primary citation

Suh, H.Y.,Lee, D.W.,Lee, K.H.,Ku, B.,Choi, S.J.,Woo, J.S.,Kim, Y.G.,Oh, B.H.
Structural Insights Into the Dual Nucleotide Exchange and Gdi Displacement Activity of Sidm/Drra
Embo J., 29:496-, 2010

PubMed Abstract: GDP-bound prenylated Rabs, sequestered by GDI (GDP dissociation inhibitor) in the cytosol, are delivered to destined sub-cellular compartment and subsequently activated by GEFs (guanine nucleotide exchange factors) catalysing GDP-to-GTP exchange. The dissociation of GDI from Rabs is believed to require a GDF (GDI displacement factor). Only two RabGDFs, human PRA-1 and Legionella pneumophila SidM/DrrA, have been identified so far and the molecular mechanism of GDF is elusive. Here, we present the structure of a SidM/DrrA fragment possessing dual GEF and GDF activity in complex with Rab1. SidM/DrrA reconfigures the Switch regions of the GTPase domain of Rab1, as eukaryotic GEFs do toward cognate Rabs. Structure-based mutational analyses show that the surface of SidM/DrrA, catalysing nucleotide exchange, is involved in GDI1 displacement from prenylated Rab1:GDP. In comparison with an eukaryotic GEF TRAPP I, this bacterial GEF/GDF exhibits high binding affinity for Rab1 with GDP retained at the active site, which appears as the key feature for the GDF activity of the protein.

PubMed: 19942850
DOI: 10.1038/EMBOJ.2009.347

Experimental method

X-RAY DIFFRACTION (1.5 Å)