1W7P

The crystal structure of endosomal complex ESCRT-II (VPS22/VPS25/VPS36)

Summary for 1W7P

• Entry DOI: 10.2210/pdb1w7p/pdb
• Related: 1U5T
• Descriptor: VPS22, YPL002C, VPS25, YJR102C, VPS36P, YLR417W (3 entities in total)
• Functional Keywords: escrt-ii complex, endosomal protein sorting, protein transport
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); More
• Cellular location: Cytoplasm : Q12483 P47142 Q06696
• Total number of polymer chains: 4
• Total formula weight: 138245.80

Authors

Teo, H.,Perisic, O.,Gonzalez, B.,Williams, R.L. (deposition date: 2004-09-07, release date: 2004-09-29, Last modification date: 2024-05-08)

Primary citation

Teo, H.,Perisic, O.,Gonzalez, B.,Williams, R.L.
Escrt-II, an Endosome-Associated Complex Required for Protein Sorting: Crystal Structure and Interactions with Escrt-III and Membranes
Dev.Cell, 7:559-, 2004

PubMed Abstract: ESCRT-I, -II, and -III protein complexes are sequentially recruited to endosomal membranes, where they orchestrate protein sorting and MVB biogenesis. In addition, they play a critical role in retrovirus budding. Structural understanding of ESCRT interaction networks is largely lacking. The 3.6 A structure of the yeast ESCRT-II core presented here reveals a trilobal complex containing two copies of Vps25, one copy of Vps22, and the C-terminal region of Vps36. Unexpectedly, the entire ESCRT-II core consists of eight repeats of a common building block, a "winged helix" domain. Two PPXY-motifs from Vps25 are involved in contacts with Vps22 and Vps36, and their mutation leads to ESCRT-II disruption. We show that purified ESCRT-II binds directly to the Vps20 component of ESCRT-III. Surprisingly, this binding does not require the protruding N-terminal coiled-coil of Vps22. Vps25 is the chief subunit responsible for Vps20 recruitment. This interaction dramatically increases binding of both components to lipid vesicles in vitro.

PubMed: 15469844
DOI: 10.1016/J.DEVCEL.2004.09.003

Experimental method

X-RAY DIFFRACTION (3.6 Å)