1NWM

GAT domain of human GGA1

Summary for 1NWM

• Entry DOI: 10.2210/pdb1nwm/pdb
• Descriptor: ADP-ribosylation factor binding protein GGA1 (2 entities in total)
• Functional Keywords: three-alpha helical bundle, 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: 16133.30

Authors

Suer, S.,Misra, S.,Saidi, L.F.,Hurley, J.H. (deposition date: 2003-02-06, release date: 2003-03-25, Last modification date: 2024-02-14)

Primary citation

Suer, S.,Misra, S.,Saidi, L.F.,Hurley, J.H.
Structure of the GAT domain of human GGA1: a syntaxin amino-terminal domain fold in an endosomal trafficking adaptor.
Proc.Natl.Acad.Sci.USA, 100:4451-4456, 2003

PubMed Abstract: The Golgi-associated, gamma-adaptin homologous, ADP-ribosylation factor (ARF)-interacting proteins (GGAs) are adaptors that sort receptors from the trans-Golgi network into the endosomallysosomal pathway. The GGAs and TOM1 (GAT) domains of the GGAs are responsible for their ARF-dependent localization. The 2.4-A crystal structure of the GAT domain of human GGA1 reveals a three-helix bundle, with a long N-terminal helical extension that is not conserved in GAT domains that do not bind ARF. The ARF binding site is located in the N-terminal extension and is separate from the core three-helix bundle. An unanticipated structural similarity to the N-terminal domain of syntaxin 1a was discovered, comprising the entire three-helix bundle. A conserved binding site on helices 2 and 3 of the GAT domain three-helix bundle is predicted to interact with coiled-coil-containing proteins. We propose that the GAT domain is descended from the same ancestor as the syntaxin 1a N-terminal domain, and that both protein families share a common function in binding coiled-coil domain proteins.

PubMed: 12668765
DOI: 10.1073/pnas.0831133100

Experimental method

X-RAY DIFFRACTION (2.4 Å)