2ZME

Integrated structural and functional model of the human ESCRT-II complex

Summary for 2ZME

• Entry DOI: 10.2210/pdb2zme/pdb
• Related: 3CUQ
• Descriptor: Vacuolar-sorting protein SNF8, Vacuolar protein-sorting-associated protein 36, Vacuolar protein-sorting-associated protein 25, ... (4 entities in total)
• Functional Keywords: escrt, sorting, mbv, vps, nucleus, protein transport, transcription, transcription regulation, transport, endosome, lipid-binding
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: Q96H20 Q86VN1 Q9BRG1
• Total number of polymer chains: 4
• Total formula weight: 80133.12

Authors

Im, Y.J.,Hurley, J.H. (deposition date: 2008-04-17, release date: 2008-11-04, Last modification date: 2023-11-01)

Primary citation

Im, Y.J.,Hurley, J.H.
Integrated structural model and membrane targeting mechanism of the human ESCRT-II complex
Dev.Cell, 14:902-913, 2008

PubMed Abstract: ESCRT-II plays a pivotal role in receptor downregulation and multivesicular body biogenesis and is conserved from yeast to humans. The crystal structures of two human ESCRT-II complex structures have been determined at 2.6 and 2.9 A resolution, respectively. The complex has three lobes and contains one copy each of VPS22 and VPS36 and two copies of VPS25. The structure reveals a dynamic helical domain to which both the VPS22 and VPS36 subunits contribute that connects the GLUE domain to the rest of the ESCRT-II core. Hydrodynamic analysis shows that intact ESCRT-II has a compact, closed conformation. ESCRT-II binds to the ESCRT-I VPS28 C-terminal domain subunit through a helix immediately C-terminal to the VPS36-GLUE domain. ESCRT-II is targeted to endosomal membranes by the lipid-binding activities of both the Vps36 GLUE domain and the first helix of Vps22. These data provide a unifying structural and functional framework for the ESCRT-II complex.

PubMed: 18539118
DOI: 10.1016/j.devcel.2008.04.004

Experimental method

X-RAY DIFFRACTION (2.9 Å)