1EO6
CRYSTAL STRUCTURE OF GATE-16
Summary for 1EO6
| Entry DOI | 10.2210/pdb1eo6/pdb |
| Descriptor | GOLGI-ASSOCIATED ATPASE ENHANCER OF 16 KD (2 entities in total) |
| Functional Keywords | ubiquitin fold, protein binding |
| Biological source | Bos taurus (cattle) |
| Total number of polymer chains | 2 |
| Total formula weight | 27373.67 |
| Authors | Paz, Y.,Elazar, Z.,Fass, D. (deposition date: 2000-03-22, release date: 2000-09-08, Last modification date: 2024-02-07) |
| Primary citation | Paz, Y.,Elazar, Z.,Fass, D. Structure of GATE-16, membrane transport modulator and mammalian ortholog of autophagocytosis factor Aut7p. J.Biol.Chem., 275:25445-25450, 2000 Cited by PubMed Abstract: The GATE-16 protein participates in intra-Golgi transport and can associate with the N-ethylmaleimide-sensitive fusion protein and with Golgi SNAREs. The yeast ortholog of GATE-16 is the autophagocytosis factor Aut7p. GATE-16 is also closely related to the GABA receptor-associated protein (GABARAP), which has been proposed to cluster neurotransmitter receptors by mediating interaction with the cytoskeleton, and to the light chain-3 subunit of the neuronal microtubule-associated protein complex. Here, we present the crystal structure of GATE-16 refined to 1.8 A resolution. GATE-16 contains a ubiquitin fold decorated by two additional N-terminal helices. Proteins with strong structural similarity but no detectable sequence homology to GATE-16 include Ras effectors that mediate diverse downstream functions, but each interacts with Ras by forming pseudo-continuous beta-sheets. The GATE-16 surface suggests that it binds its targets in a similar manner. Moreover, a second potential protein-protein interaction site on GATE-16 may explain the adapter activity observed for members of the GATE-16 family. PubMed: 10856287DOI: 10.1074/jbc.C000307200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
Download full validation report
