1j2j

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spinqualitylabelsall models 1j2j, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of GGA1 GAT N-terminal region in complex with ARF1 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

1J2J is a Protein complex structure of sequences from Homo sapiens and Mus musculus with MG, IOD and GTP as ligands. 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

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