2caz: Difference between revisions

Revision as of 17:46, 21 February 2008

ESCRT-I CORE

OverviewOverview

ESCRT complexes form the main machinery driving protein sorting from endosomes to lysosomes. Currently, the picture regarding assembly of ESCRTs on endosomes is incomplete. The structure of the conserved heterotrimeric ESCRT-I core presented here shows a fan-like arrangement of three helical hairpins, each corresponding to a different subunit. Vps23/Tsg101 is the central hairpin sandwiched between the other subunits, explaining the critical role of its "steadiness box" in the stability of ESCRT-I. We show that yeast ESCRT-I links directly to ESCRT-II, through a tight interaction of Vps28 (ESCRT-I) with the yeast-specific zinc-finger insertion within the GLUE domain of Vps36 (ESCRT-II). The crystal structure of the GLUE domain missing this insertion reveals it is a split PH domain, with a noncanonical lipid binding pocket that binds PtdIns3P. The simultaneous and reinforcing interactions of ESCRT-II GLUE domain with membranes, ESCRT-I, and ubiquitin are critical for ubiquitinated cargo progression from early to late endosomes.

About this StructureAbout this Structure

2CAZ is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

ESCRT-I core and ESCRT-II GLUE domain structures reveal role for GLUE in linking to ESCRT-I and membranes., Teo H, Gill DJ, Sun J, Perisic O, Veprintsev DB, Vallis Y, Emr SD, Williams RL, Cell. 2006 Apr 7;125(1):99-111. PMID:16615893

Page seeded by OCA on Thu Feb 21 16:46:51 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:2caz.gif|left|200px]]<br /><applet load="2caz" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2caz.gif|left|200px]]<br /><applet load="2caz" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2caz, resolution 3.60&Aring;" />
 '''ESCRT-I CORE'''<br />
 ==Overview==
-ESCRT complexes form the main machinery driving protein sorting from, endosomes to lysosomes. Currently, the picture regarding assembly of, ESCRTs on endosomes is incomplete. The structure of the conserved, heterotrimeric ESCRT-I core presented here shows a fan-like arrangement of, three helical hairpins, each corresponding to a different subunit., Vps23/Tsg101 is the central hairpin sandwiched between the other subunits, explaining the critical role of its "steadiness box" in the stability of, ESCRT-I. We show that yeast ESCRT-I links directly to ESCRT-II, through a, tight interaction of Vps28 (ESCRT-I) with the yeast-specific zinc-finger, insertion within the GLUE domain of Vps36 (ESCRT-II). The crystal, structure of the GLUE domain missing this insertion reveals it is a split, PH domain, with a noncanonical lipid binding pocket that binds PtdIns3P., The simultaneous and reinforcing interactions of ESCRT-II GLUE domain with, membranes, ESCRT-I, and ubiquitin are critical for ubiquitinated cargo, progression from early to late endosomes.
+ESCRT complexes form the main machinery driving protein sorting from endosomes to lysosomes. Currently, the picture regarding assembly of ESCRTs on endosomes is incomplete. The structure of the conserved heterotrimeric ESCRT-I core presented here shows a fan-like arrangement of three helical hairpins, each corresponding to a different subunit. Vps23/Tsg101 is the central hairpin sandwiched between the other subunits, explaining the critical role of its "steadiness box" in the stability of ESCRT-I. We show that yeast ESCRT-I links directly to ESCRT-II, through a tight interaction of Vps28 (ESCRT-I) with the yeast-specific zinc-finger insertion within the GLUE domain of Vps36 (ESCRT-II). The crystal structure of the GLUE domain missing this insertion reveals it is a split PH domain, with a noncanonical lipid binding pocket that binds PtdIns3P. The simultaneous and reinforcing interactions of ESCRT-II GLUE domain with membranes, ESCRT-I, and ubiquitin are critical for ubiquitinated cargo progression from early to late endosomes.
 ==About this Structure==
-CAZ 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=2CAZ OCA].
+CAZ 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=2CAZ OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Protein complex]]
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Emr, S.D.]]
+[[Category: Emr, S D.]]
-[[Category: Gill, D.J.]]
+[[Category: Gill, D J.]]
 [[Category: Perisic, O.]]
 [[Category: Sun, J.]]
 [[Category: Teo, H.]]
 [[Category: Vallis, Y.]]
-[[Category: Veprintsev, D.B.]]
+[[Category: Veprintsev, D B.]]
-[[Category: Williams, R.L.]]
+[[Category: Williams, R L.]]
 [[Category: coiled coil]]
 [[Category: endosome]]
@@ Line 40: / Line 40: @@
 [[Category: vps37]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:04:01 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:46:51 2008''