1w7p
From Proteopedia
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THE CRYSTAL STRUCTURE OF ENDOSOMAL COMPLEX ESCRT-II (VPS22/VPS25/VPS36)
Overview
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.
About this Structure
1W7P is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
ESCRT-II, an endosome-associated complex required for protein sorting: crystal structure and interactions with ESCRT-III and membranes., Teo H, Perisic O, Gonzalez B, Williams RL, Dev Cell. 2004 Oct;7(4):559-69. PMID:15469844
Page seeded by OCA on Wed Nov 21 05:15:13 2007
