1w7p
From Proteopedia
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| - | [[Image:1w7p.jpg|left|200px]] | + | [[Image:1w7p.jpg|left|200px]] |
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| - | '''THE CRYSTAL STRUCTURE OF ENDOSOMAL COMPLEX ESCRT-II (VPS22/VPS25/VPS36)''' | + | {{Structure |
| + | |PDB= 1w7p |SIZE=350|CAPTION= <scene name='initialview01'>1w7p</scene>, resolution 3.60Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''THE CRYSTAL STRUCTURE OF ENDOSOMAL COMPLEX ESCRT-II (VPS22/VPS25/VPS36)''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1W7P is a [ | + | 1W7P is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W7P OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15469844 15469844] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
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[[Category: vps36]] | [[Category: vps36]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:53:18 2008'' |
Revision as of 12:53, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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