3NS4
Structure of a C-terminal fragment of its Vps53 subunit suggests similarity of GARP to a family of tethering complexes
Summary for 3NS4
| Entry DOI | 10.2210/pdb3ns4/pdb |
| Descriptor | Vacuolar protein sorting-associated protein 53, BARIUM ION (3 entities in total) |
| Functional Keywords | garp complex component, helical bundle, membrane tethering complex, membrane traffic, vps51, vps52, vps54, arl1, protein binding |
| Biological source | Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast) |
| Cellular location | Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein: P47061 |
| Total number of polymer chains | 1 |
| Total formula weight | 32300.33 |
| Authors | Vasan, N.,Reinisch, K.M. (deposition date: 2010-07-01, release date: 2010-09-15, Last modification date: 2024-10-09) |
| Primary citation | Vasan, N.,Hutagalung, A.,Novick, P.,Reinisch, K.M. Structure of a C-terminal fragment of its Vps53 subunit suggests similarity of Golgi-associated retrograde protein (GARP) complex to a family of tethering complexes. Proc.Natl.Acad.Sci.USA, 107:14176-14181, 2010 Cited by PubMed Abstract: The Golgi-associated retrograde protein (GARP) complex is a membrane-tethering complex that functions in traffic from endosomes to the trans-Golgi network. Here we present the structure of a C-terminal fragment of the Vps53 subunit, important for binding endosome-derived vesicles, at a resolution of 2.9 A. We show that the C terminus consists of two alpha-helical bundles arranged in tandem, and we identify a highly conserved surface patch, which may play a role in vesicle recognition. Mutations of the surface result in defects in membrane traffic. The fold of the Vps53 C terminus is strongly reminiscent of proteins that belong to three other tethering complexes--Dsl1, conserved oligomeric Golgi, and the exocyst--thought to share a common evolutionary origin. Thus, the structure of the Vps53 C terminus suggests that GARP belongs to this family of complexes. PubMed: 20660722DOI: 10.1073/pnas.1009419107 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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