1w7p
From Proteopedia
(New page: 200px<br /><applet load="1w7p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1w7p, resolution 3.60Å" /> '''THE CRYSTAL STRUCTUR...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1w7p.jpg|left|200px]]<br /><applet load="1w7p" size=" | + | [[Image:1w7p.jpg|left|200px]]<br /><applet load="1w7p" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1w7p, resolution 3.60Å" /> | caption="1w7p, resolution 3.60Å" /> | ||
'''THE CRYSTAL STRUCTURE OF ENDOSOMAL COMPLEX ESCRT-II (VPS22/VPS25/VPS36)'''<br /> | '''THE CRYSTAL STRUCTURE OF ENDOSOMAL COMPLEX ESCRT-II (VPS22/VPS25/VPS36)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | ESCRT-I, -II, and -III protein complexes are sequentially recruited to | + | 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== | ==About this Structure== | ||
| - | 1W7P is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http:// | + | 1W7P is a [http://en.wikipedia.org/wiki/Protein_complex 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== | ||
| Line 16: | Line 16: | ||
[[Category: Perisic, O.]] | [[Category: Perisic, O.]] | ||
[[Category: Teo, H.]] | [[Category: Teo, H.]] | ||
| - | [[Category: Williams, R | + | [[Category: Williams, R L.]] |
[[Category: endosomal protein sorting]] | [[Category: endosomal protein sorting]] | ||
[[Category: escrt-ii complex]] | [[Category: escrt-ii complex]] | ||
| Line 24: | Line 24: | ||
[[Category: vps36]] | [[Category: vps36]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:41:19 2008'' |
Revision as of 13:41, 21 February 2008
|
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 Thu Feb 21 15:41:19 2008
