1O3Y

Crystal structure of mouse ARF1 (delta17-Q71L), GTP form

Replaces:  1J2I

Summary for 1O3Y

• Entry DOI: 10.2210/pdb1o3y/pdb
• Related: 1J2H 1J2J
• Descriptor: ADP-ribosylation factor 1, MAGNESIUM ION, GUANOSINE-5'-TRIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: protein transport
• Biological source: Mus musculus (house mouse)
• Cellular location: Golgi apparatus: P84078
• Total number of polymer chains: 2
• Total formula weight: 38998.20

Authors

Shiba, T.,Kawasaki, M.,Takatsu, H.,Nogi, T.,Matsugaki, N.,Igarashi, N.,Suzuki, M.,Kato, R.,Nakayama, K.,Wakatsuki, S. (deposition date: 2003-05-08, release date: 2003-05-20, Last modification date: 2023-10-25)

Primary citation

Shiba, T.,Kawasaki, M.,Takatsu, H.,Nogi, T.,Matsugaki, N.,Igarashi, N.,Suzuki, M.,Kato, R.,Nakayama, K.,Wakatsuki, S.
Molecular mechanism of membrane recruitment of GGA by ARF in lysosomal protein transport
Nat.Struct.Biol., 10:386-393, 2003

PubMed Abstract: GGAs are critical for trafficking soluble proteins from the trans-Golgi network (TGN) to endosomes/lysosomes through interactions with TGN-sorting receptors, ADP-ribosylation factor (ARF) and clathrin. ARF-GTP bound to TGN membranes recruits its effector GGA by binding to the GAT domain, thus facilitating recognition of GGA for cargo-loaded receptors. Here we report the X-ray crystal structures of the human GGA1-GAT domain and the complex between ARF1-GTP and the N-terminal region of the GAT domain. When unbound, the GAT domain forms an elongated bundle of three a-helices with a hydrophobic core. Structurally, this domain, combined with the preceding VHS domain, resembles CALM, an AP180 homolog involved in endocytosis. In the complex with ARF1-GTP, a helix-loop-helix of the N-terminal part of GGA1-GAT interacts with the switches 1 and 2 of ARF1 predominantly in a hydrophobic manner. These data reveal a molecular mechanism underlying membrane recruitment of adaptor proteins by ARF-GTP.

PubMed: 12679809
DOI: 10.1038/nsb920

Experimental method

X-RAY DIFFRACTION (1.5 Å)