2F6M

Structure of a Vps23-C:Vps28-N subcomplex

Summary for 2F6M

• Entry DOI: 10.2210/pdb2f6m/pdb
• Related: 1u5t 1uzx 1w7p 1xb4 2f66
• Descriptor: Suppressor protein STP22 of temperature-sensitive alpha-factor receptor and arginine permease, Vacuolar protein sorting-associated protein VPS28, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: endosomes, trafficking complex, vps23, vps28, vacuole 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
• Total number of polymer chains: 4
• Total formula weight: 41804.25

Authors

Kostelansky, M.S.,Lee, S.,Kim, J.,Hurley, J.H. (deposition date: 2005-11-29, release date: 2006-04-18, Last modification date: 2024-02-14)

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

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: 16615894
DOI: 10.1016/j.cell.2006.01.049

Experimental method

X-RAY DIFFRACTION (2.1 Å)