2J59

Crystal structure of the ARF1:ARHGAP21-ArfBD complex

Summary for 2J59

• Entry DOI: 10.2210/pdb2j59/pdb
• Related: 1O3Y
• Descriptor: ADP-RIBOSYLATION FACTOR 1, RHO-GTPASE ACTIVATING PROTEIN 10, GUANOSINE-5'-TRIPHOSPHATE, ... (8 entities in total)
• Functional Keywords: arf, arf1, arfbd, arhgap21, myristate, transport, nucleotide-binding, rhogap protein, hydrolase, protein transport, actin organization, small gtp-binding protein, golgi apparatus
• Biological source: MUS MUSCULUS (MOUSE); More
• Cellular location: Golgi apparatus: P84078
• Total number of polymer chains: 12
• Total formula weight: 234295.03

Authors

Menetrey, J.,Perderiset, M.,Cicolari, J.,Dubois, T.,El Khatib, N.,El Khadali, F.,Franco, M.,Chavrier, P.,Houdusse, A. (deposition date: 2006-09-13, release date: 2007-02-20, Last modification date: 2023-12-13)

Primary citation

Menetrey, J.,Perderiset, M.,Cicolari, J.,Dubois, T.,El Khatib, N.,El Khadali, F.,Franco, M.,Chavrier, P.,Houdusse, A.
Structural Basis for Arf1-Mediated Recruitment of Arhgap21 to Golgi Membranes.
Embo J., 26:1953-, 2007

PubMed Abstract: ARHGAP21 is a Rho family GTPase-activating protein (RhoGAP) that controls the Arp2/3 complex and F-actin dynamics at the Golgi complex by regulating the activity of the small GTPase Cdc42. ARHGAP21 is recruited to the Golgi by binding to another small GTPase, ARF1. Here, we present the crystal structure of the activated GTP-bound form of ARF1 in a complex with the Arf-binding domain (ArfBD) of ARHGAP21 at 2.1 A resolution. We show that ArfBD comprises a PH domain adjoining a C-terminal alpha helix, and that ARF1 interacts with both of these structural motifs through its switch regions and triggers structural rearrangement of the PH domain. We used site-directed mutagenesis to confirm that both the PH domain and the helical motif are essential for the binding of ArfBD to ARF1 and for its recruitment to the Golgi. Our data demonstrate that two well-known small GTPase-binding motifs, the PH domain and the alpha helical motif, can combine to create a novel mode of binding to Arfs.

PubMed: 17347647
DOI: 10.1038/SJ.EMBOJ.7601634

Experimental method

X-RAY DIFFRACTION (2.1 Å)