3MNM

Crystal structure of GAE domain of GGA2p from Saccharomyces cerevisiae

Summary for 3MNM

• Entry DOI: 10.2210/pdb3mnm/pdb
• Descriptor: ADP-ribosylation factor-binding protein GGA2, SULFATE ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: ig-like, beta sandwich, protein transport
• Biological source: Saccharomyces cerevisiae (yeast)
• Cellular location: Golgi apparatus, trans-Golgi network: P38817
• Total number of polymer chains: 3
• Total formula weight: 41012.46

Authors

Fang, P.,Wang, J.,Li, X.,Niu, L.,Teng, M. (deposition date: 2010-04-21, release date: 2010-09-08, Last modification date: 2025-03-26)

Primary citation

Fang, P.,Li, X.,Wang, J.,Niu, L.,Teng, M.
Structural basis for the specificity of the GAE domain of yGGA2 for its accessory proteins Ent3 and Ent5
Biochemistry, 49:7949-7955, 2010

PubMed Abstract: Different assemblies of accessory proteins with clathrin are critical for transporting precisely various cargos between intracellular compartments. GGA proteins are adaptors for clathrin-mediated intracellular trafficking, connecting other accessory and cargo proteins to clathrin-coated vesicles. Both binding to the GAE domain of GGA protein yGGA2 in Saccharomyces cerevisia, Ent3 and Ent5 are involved in different trafficking pathways. Ent5 is ubiquitous and localized in a manner independent of yGGA2, and Ent3 functions preferentially through yGGA2. Not known are the sources of these differences. Here we show not all acidic-phenylalanine motifs in Ent3/5 are active for yGGA2_GAE domain binding. Two of the three acidic-phenylalanine motifs from Ent3 can bind to the yGGA2_GAE domain, while only one of the two motifs from Ent5 can bind. We also determined the crystal structure of the yGGA2_GAE domain at 1.8 A resolution. Structural docking and mutagenesis analysis shows inactive motifs in Ent3 and Ent5 repel yGGA2_GAE binding through disfavored residues at positions 1 and 3. These results suggest accessory proteins may fine-tune the GGA adaptor dependence by adjusting their non-acidic-phenylalanine residues, thus contributing to the distinct role of Ent3 and Ent5 in trafficking.

PubMed: 20704189
DOI: 10.1021/bi1010255

Experimental method

X-RAY DIFFRACTION (1.73 Å)