1OM9

Structure of the GGA1-appendage in complex with the p56 binding peptide

Summary for 1OM9

• Entry DOI: 10.2210/pdb1om9/pdb
• Related: 1GYU 1IU1 1NA8
• Descriptor: ADP-ribosylation factor binding protein GGA1, 15-mer peptide fragment of p56 (3 entities in total)
• Functional Keywords: beta sandwich, beta augmentation, gga, adaptin, clathrin adaptor, protein transport, signaling protein
• Biological source: Homo sapiens (human); More
• Cellular location: Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein: Q9UJY5
• Total number of polymer chains: 4
• Total formula weight: 37947.37

Authors

Collins, B.M.,Praefcke, G.J.K.,Robinson, M.S.,Owen, D.J. (deposition date: 2003-02-25, release date: 2003-07-29, Last modification date: 2023-08-16)

Primary citation

Collins, B.M.,Praefcke, G.J.K.,Robinson, M.S.,Owen, D.J.
Structural basis for binding of accessory proteins by the appendage domain of GGAs
Nat.Struct.Biol., 10:607-613, 2003

PubMed Abstract: The Golgi-associated, gamma-adaptin-related, ADP-ribosylation-factor binding proteins (GGAs) and adaptor protein (AP)-1 are adaptors involved in clathrin-mediated transport between the trans-Golgi network and endosomal system. The appendage domains of GGAs and the AP-1 gamma-adaptin subunit are structurally homologous and have been proposed to bind to accessory proteins via interaction with short sequences containing phenylalanines and acidic residues. Here we present the structure of the human GGA1 appendage in complex with its cognate binding peptide from the p56 accessory protein (DDDDFGGFEAAETFD) as determined by X-ray crystallography. The interaction is governed predominantly by packing of the first two phenylalanine residues of the peptide with conserved basic and hydrophobic residues from GGA1. Additionally, several main chain hydrogen bonds cause the peptide to form an additional beta-strand on the edge of the preexisting beta-sheet of the protein. Isothermal titration calorimetry was used to assess the affinities of different peptides for the GGA and gamma-appendage domains.

PubMed: 12858163
DOI: 10.1038/nsb955

Experimental method

X-RAY DIFFRACTION (2.5 Å)