2F66
Structure of the ESCRT-I endosomal trafficking complex
Summary for 2F66
| Entry DOI | 10.2210/pdb2f66/pdb |
| Related | 1U5T 1UZX 1W7P 1XB4 |
| Descriptor | Suppressor protein STP22 of temperature-sensitive alpha-factor receptor and arginine permease, Vacuolar protein sorting-associated protein VPS28, Protein SRN2, ... (5 entities in total) |
| Functional Keywords | endosome, trafficking complex, vps23, vps28, vps37, vacuolar protein sorting, escrt protein complexes, endosomal sorting complex required for transport, escrt-i, ubiquitin, tsg101, transport protein |
| Biological source | Saccharomyces cerevisiae (baker's yeast) More |
| Cellular location | Cytoplasm: P25604 Q02767 Q99176 |
| Total number of polymer chains | 6 |
| Total formula weight | 61554.80 |
| Authors | Kostelansky, M.S.,Lee, S.,Kim, J.,Hurley, J.H. (deposition date: 2005-11-28, release date: 2006-04-18, Last modification date: 2023-08-23) |
| Primary citation | Kostelansky, M.S.,Sun, J.,Lee, S.,Kim, J.,Ghirlando, R.,Hierro, A.,Emr, S.D.,Hurley, J.H. Structural and functional organization of the ESCRT-I trafficking complex. Cell(Cambridge,Mass.), 125:113-126, 2006 Cited by PubMed Abstract: The endosomal sorting complex required for transport (ESCRT) complexes are central to receptor downregulation, lysosome biogenesis, and budding of HIV. The yeast ESCRT-I complex contains the Vps23, Vps28, and Vps37 proteins, and its assembly is directed by the C-terminal steadiness box of Vps23, the N-terminal half of Vps28, and the C-terminal half of Vps37. The crystal structures of a Vps23:Vps28 core subcomplex and the Vps23:Vps28:Vps37 core were solved at 2.1 and 2.8 A resolution. Each subunit contains a structurally similar pair of helices that form the core. The N-terminal domain of Vps28 has a hydrophobic binding site on its surface that is conformationally dynamic. The C-terminal domain of Vps28 binds the ESCRT-II complex. The structure shows how ESCRT-I is assembled by a compact core from which the Vps23 UEV domain, the Vps28 C domain, and other domains project to bind their partners. PubMed: 16615894DOI: 10.1016/j.cell.2006.01.049 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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