1w7p: Difference between revisions

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[[Image:1w7p.jpg|left|200px]]<br /><applet load="1w7p" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1w7p.jpg|left|200px]]<br /><applet load="1w7p" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1w7p, resolution 3.60Å" />

'''THE CRYSTAL STRUCTURE OF ENDOSOMAL COMPLEX ESCRT-II (VPS22/VPS25/VPS36)'''<br />

==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.

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 [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].

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==

Line 16:

[[Category: Perisic, O.]]

[[Category: Teo, H.]]

[[Category: Williams, R.L.]]

[[Category: Williams, R L.]]

[[Category: endosomal protein sorting]]

[[Category: escrt-ii complex]]

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[[Category: vps36]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:41:19 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1w7p.jpg|left|200px]]<br /><applet load="1w7p" size="450" color="white" frame="true" align="right" spinBox="true"
+[[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;" />
 '''THE CRYSTAL STRUCTURE OF ENDOSOMAL COMPLEX ESCRT-II (VPS22/VPS25/VPS36)'''<br />
 ==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.
+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==
-W7P 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].
+W7P 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==
@@ Line 16: / Line 16: @@
 [[Category: Perisic, O.]]
 [[Category: Teo, H.]]
-[[Category: Williams, R.L.]]
+[[Category: Williams, R L.]]
 [[Category: endosomal protein sorting]]
 [[Category: escrt-ii complex]]
@@ Line 24: / Line 24: @@
 [[Category: vps36]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:15:13 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:41:19 2008''