4DCN

Crystal Structure Analysis of the Arfaptin2 BAR domain in Complex with ARL1

Summary for 4DCN

• Entry DOI: 10.2210/pdb4dcn/pdb
• Related: 1I49 1I4L 1MOZ 1UPT 3DYT
• Descriptor: ADP-ribosylation factor-like protein 1, Arfaptin-2, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: small gtpase effector complex, bar domain, membrane deformation, protein binding-signaling protein complex, protein binding/signaling protein
• Biological source: Homo sapiens (human); More
• Cellular location: Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side: P40616
• Total number of polymer chains: 4
• Total formula weight: 83649.32

Authors

Nakamura, K.,Xie, Y.,Kawasaki, M.,Kato, R.,Wakatsuki, S. (deposition date: 2012-01-18, release date: 2012-06-13, Last modification date: 2024-03-20)

Primary citation

Nakamura, K.,Man, Z.,Xie, Y.,Hanai, A.,Makyio, H.,Kawasaki, M.,Kato, R.,Shin, H.-W.,Nakayama, K.,Wakatsuki, S.
Structural basis for membrane binding specificity of the Bin/Amphiphysin/Rvs (BAR) domain of Arfaptin-2 determined by Arl1 GTPase
J.Biol.Chem., 287:25478-25489, 2012

PubMed Abstract: Membrane-sculpting BAR (Bin/Amphiphysin/Rvs) domains form a crescent-shaped homodimer that can sense and induce membrane curvature through its positively charged concave face. We have recently shown that Arfaptin-2, which was originally identified as a binding partner for the Arf and Rac1 GTPases, binds to Arl1 through its BAR domain and is recruited onto Golgi membranes. There, Arfaptin-2 induces membrane tubules. Here, we report the crystal structure of the Arfaptin-2 BAR homodimer in complex with two Arl1 molecules bound symmetrically to each side, leaving the concave face open for membrane association. The overall structure of the Arl1·Arfaptin-2 BAR complex closely resembles that of the PX-BAR domain of sorting nexin 9, suggesting similar mechanisms underlying BAR domain targeting to specific organellar membranes. The Arl1·Arfaptin-2 BAR structure suggests that one of the two Arl1 molecules competes with Rac1, which binds to the concave face of the Arfaptin-2 BAR homodimer and may hinder its membrane association.

PubMed: 22679020
DOI: 10.1074/jbc.M112.365783

Experimental method

X-RAY DIFFRACTION (3.01 Å)