1P4U

CRYSTAL STRUCTURE OF GGA3 GAE DOMAIN IN COMPLEX WITH RABAPTIN-5 PEPTIDE

Summary for 1P4U

• Entry DOI: 10.2210/pdb1p4u/pdb
• Descriptor: ADP-ribosylation factor binding protein GGA3, Rabaptin-5 (3 entities in total)
• Functional Keywords: protein transport
• Biological source: Homo sapiens (human); More
• Cellular location: Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein: Q9NZ52; Cytoplasm: Q15276
• Total number of polymer chains: 2
• Total formula weight: 17838.69

Authors

Miller, G.J.,Mattera, R.,Bonifacino, J.S.,Hurley, J.H. (deposition date: 2003-04-24, release date: 2003-07-29, Last modification date: 2024-02-14)

Primary citation

MILLER, G.J.,MATTERA, R.,BONIFACINO, J.S.,HURLEY, J.H.
RECOGNITION OF ACCESSORY PROTEIN MOTIFS BY THE GAMMA-ADAPTIN EAR DOMAIN OF GGA3
Nat.Struct.Biol., 10:599-606, 2003

PubMed Abstract: Adaptor proteins load transmembrane protein cargo into transport vesicles and serve as nexuses for the formation of large multiprotein complexes on the nascent vesicles. The gamma-adaptin ear (GAE) domains of the AP-1 adaptor protein complex and the GGA adaptor proteins recruit accessory proteins to these multiprotein complexes by binding to a hydrophobic motif. We determined the structure of the GAE domain of human GGA3 in complex with a peptide based on the DFGPLV sequence of the accessory protein Rabaptin-5 and refined it at a resolution of 2.2 A. The leucine and valine residues of the peptide are partly buried in two contiguous shallow, hydrophobic depressions. The anchoring phenylalanine is buried in a deep pocket formed by the aliphatic portions of two conserved arginine residues, along with an alanine and a proline, illustrating the unusual function of a cluster of basic residues in binding a hydrophobic motif.

PubMed: 12858162
DOI: 10.1038/nsb953

Experimental method

X-RAY DIFFRACTION (2.2 Å)