1NAF

Crystal structure of the human GGA1 GAT domain

Summary for 1NAF

• Entry DOI: 10.2210/pdb1naf/pdb
• Related: 1GYU 1NA8
• Descriptor: ADP-ribosylation factor binding protein GGA1 (1 entity in total)
• Functional Keywords: clathrin-adaptor, gga, gat domain, helical paper-clip, three-helix bundle, signaling protein, membrane protein
• 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: 18412.45

Authors

Collins, B.M.,Watson, P.J.,Owen, D.J. (deposition date: 2002-11-27, release date: 2003-03-25, Last modification date: 2024-10-16)

Primary citation

Collins, B.M.,Watson, P.J.,Owen, D.J.
The Structure of the GGA1-GAT Domain Reveals the Molecular Basis for ARF Binding and Membrane Association of GGAs
Dev.Cell, 4:321-332, 2003

PubMed Abstract: The GGAs are a family of clathrin adaptor proteins involved in vesicular transport between the trans-Golgi network and endosomal system. Here we confirm reports that GGAs are targeted to the Golgi via interaction between the GGA-GAT domain and ARF-GTP, and we present the structure of the GAT domain of human GGA1, completing the structural description of the folded domains of GGA proteins. The GGA-GAT domain possesses an all alpha-helical fold with a "paper clip" topology comprising two independent subdomains. Structure-based mutagenesis demonstrates that ARF1-GTP binding by GGAs is exclusively governed by the N-terminal "hook" subdomain, and, using an in vitro recruitment assay, we show that ARF-GTP binding by this small structure is required and sufficient for Golgi targeting of GGAs.

PubMed: 12636914
DOI: 10.1016/S1534-5807(03)00037-6

Experimental method

X-RAY DIFFRACTION (2.8 Å)