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1NAF

Crystal structure of the human GGA1 GAT domain

Summary for 1NAF
Entry DOI10.2210/pdb1naf/pdb
Related1GYU 1NA8
DescriptorADP-ribosylation factor binding protein GGA1 (1 entity in total)
Functional Keywordsclathrin-adaptor, gga, gat domain, helical paper-clip, three-helix bundle, signaling protein, membrane protein
Biological sourceHomo sapiens (human)
Cellular locationGolgi apparatus, trans-Golgi network membrane; Peripheral membrane protein: Q9UJY5
Total number of polymer chains1
Total formula weight18412.45
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 citationCollins, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.8 Å)
Structure validation

238582

数据于2025-07-09公开中

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