1o3y
Crystal structure of mouse ARF1 (delta17-Q71L), GTP form
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OverviewOverview
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 StructureAbout this Structure
1O3Y is a Single protein structure of sequence from Mus musculus with MG and GTP as ligands. This structure superseeds the now removed PDB entry 1J2I. Full crystallographic information is available from OCA.
ReferenceReference
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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