3HTU
Crystal structure of the human VPS25-VPS20 subcomplex
Summary for 3HTU
| Entry DOI | 10.2210/pdb3htu/pdb |
| Descriptor | Vacuolar protein-sorting-associated protein 25, Vacuolar protein-sorting-associated protein 20 (3 entities in total) |
| Functional Keywords | escrt-ii, escrt-iii, vps20, vps25, mvb, cytoplasm, nucleus, polymorphism, protein transport, transcription, transcription regulation, transport, coiled coil, endosome, lipoprotein, membrane, myristate |
| Biological source | Homo sapiens (human) More |
| Cellular location | Cytoplasm: Q9BRG1 Endomembrane system: Q96FZ7 |
| Total number of polymer chains | 8 |
| Total formula weight | 54917.29 |
| Authors | Im, Y.J.,Hurley, J.H. (deposition date: 2009-06-12, release date: 2009-08-25, Last modification date: 2023-09-06) |
| Primary citation | Im, Y.J.,Wollert, T.,Boura, E.,Hurley, J.H. Structure and function of the ESCRT-II-III interface in multivesicular body biogenesis. Dev.Cell, 17:234-243, 2009 Cited by PubMed Abstract: The ESCRT-II-ESCRT-III interaction coordinates the sorting of ubiquitinated cargo with the budding and scission of intralumenal vesicles into multivesicular bodies. The interacting regions of these complexes were mapped to the second winged helix domain of human ESCRT-II subunit VPS25 and the first helix of ESCRT-III subunit VPS20. The crystal structure of this complex was determined at 2.0 A resolution. Residues involved in structural interactions explain the specificity of ESCRT-II for Vps20, and are critical for cargo sorting in vivo. ESCRT-II directly activates ESCRT-III-driven vesicle budding and scission in vitro via these structural interactions. VPS20 and ESCRT-II bind membranes with nanomolar affinity, explaining why binding to ESCRT-II is dispensable for the recruitment of Vps20 to membranes. Docking of the ESCRT-II-VPS20(2) supercomplex reveals a convex membrane-binding surface, suggesting a hypothesis for negative membrane curvature induction in the nascent intralumenal vesicle. PubMed: 19686684DOI: 10.1016/j.devcel.2009.07.008 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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