2P22
Structure of the Yeast ESCRT-I Heterotetramer Core
Summary for 2P22
| Entry DOI | 10.2210/pdb2p22/pdb |
| Related | 1UZX 2CAZ 2F66 2F6M 2J9U 2J9V |
| Descriptor | Suppressor protein STP22 of temperature-sensitive alpha-factor receptor and arginine permease, Vacuolar protein sorting-associated protein 28, Protein SRN2, ... (6 entities in total) |
| Functional Keywords | endosome, trafficking complex, vps23, vps28, vps37, mvb12, 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 |
| Total number of polymer chains | 4 |
| Total formula weight | 66302.47 |
| Authors | Kostelansky, M.S.,Hurley, J.H. (deposition date: 2007-03-06, release date: 2007-06-05, Last modification date: 2024-02-21) |
| Primary citation | Kostelansky, M.S.,Schluter, C.,Tam, Y.Y.,Lee, S.,Ghirlando, R.,Beach, B.,Conibear, E.,Hurley, J.H. Molecular architecture and functional model of the complete yeast ESCRT-I heterotetramer. Cell(Cambridge,Mass.), 129:485-498, 2007 Cited by PubMed Abstract: The endosomal sorting complex required for transport-I (ESCRT-I) complex, which is conserved from yeast to humans, directs the lysosomal degradation of ubiquitinated transmembrane proteins and the budding of the HIV virus. Yeast ESCRT-I contains four subunits, Vps23, Vps28, Vps37, and Mvb12. The crystal structure of the heterotetrameric ESCRT-I complex reveals a highly asymmetric complex of 1:1:1:1 subunit stoichiometry. The core complex is nearly 18 nm long and consists of a headpiece attached to a 13 nm stalk. The stalk is important for cargo sorting by ESCRT-I and is proposed to serve as a spacer regulating the correct disposition of cargo and other ESCRT components. Hydrodynamic constraints and crystallographic structures were used to generate a model of intact ESCRT-I in solution. The results show how ESCRT-I uses a combination of a rigid stalk and flexible tethers to interact with lipids, cargo, and other ESCRT complexes over a span of approximately 25 nm. PubMed: 17442384DOI: 10.1016/j.cell.2007.03.016 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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