Summary for 1O3X
| Entry DOI | 10.2210/pdb1o3x/pdb |
| Related | 1J2I 1J2J |
| Descriptor | ADP-ribosylation factor binding protein GGA1 (2 entities in total) |
| Functional Keywords | protein transport |
| Biological source | Homo sapiens (human) |
| Cellular location | Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein: Q9UJY5 |
| Total number of polymer chains | 1 |
| Total formula weight | 16000.13 |
| 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: 2023-12-27) |
| 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 Cited by 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: 12679809DOI: 10.1038/nsb920 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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