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1w7p

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(New page: 200px<br /><applet load="1w7p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1w7p, resolution 3.60&Aring;" /> '''THE CRYSTAL STRUCTUR...)
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[[Image:1w7p.jpg|left|200px]]<br /><applet load="1w7p" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1w7p, resolution 3.60&Aring;" />
caption="1w7p, resolution 3.60&Aring;" />
'''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==
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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.
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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1W7P OCA].
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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==
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[[Category: Perisic, O.]]
[[Category: Perisic, O.]]
[[Category: Teo, H.]]
[[Category: Teo, H.]]
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[[Category: Williams, R.L.]]
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[[Category: Williams, R L.]]
[[Category: endosomal protein sorting]]
[[Category: endosomal protein sorting]]
[[Category: escrt-ii complex]]
[[Category: escrt-ii complex]]
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[[Category: vps36]]
[[Category: vps36]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:15:13 2007''
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''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


1w7p, resolution 3.60Å

Drag the structure with the mouse to rotate

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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