1o3y
From Proteopedia
Crystal structure of mouse ARF1 (delta17-Q71L), GTP form
Overview
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.
About this Structure
1O3Y is a Single protein structure of sequence from Mus musculus. This structure supersedes the now removed PDB entry 1j2i. Full crystallographic information is available from OCA.
Reference
Molecular mechanism of membrane recruitment of GGA by ARF in lysosomal protein transport., Shiba T, Kawasaki M, Takatsu H, Nogi T, Matsugaki N, Igarashi N, Suzuki M, Kato R, Nakayama K, Wakatsuki S, Nat Struct Biol. 2003 May;10(5):386-93. PMID:12679809 Page seeded by OCA on Sat May 3 03:21:24 2008
