2cay

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[[Image:2cay.gif|left|200px]]<br /><applet load="2cay" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2cay.gif|left|200px]]
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caption="2cay, resolution 1.90&Aring;" />
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'''VPS36 N-TERMINAL PH DOMAIN'''<br />
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{{Structure
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|PDB= 2cay |SIZE=350|CAPTION= <scene name='initialview01'>2cay</scene>, resolution 1.90&Aring;
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|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+B'>AC1</scene>
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|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''VPS36 N-TERMINAL PH DOMAIN'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2CAY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CAY OCA].
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2CAY is a [[Single protein]] structure of sequence 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=2CAY OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16615893 16615893]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/16615893 16615893]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: membrane]]
[[Category: membrane]]
[[Category: metal-binding]]
[[Category: metal-binding]]
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[[Category: multivesicular bodies]]
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[[Category: multivesicular body]]
[[Category: ph domain]]
[[Category: ph domain]]
[[Category: protein transport]]
[[Category: protein transport]]
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[[Category: zinc-finger]]
[[Category: zinc-finger]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:46:51 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:13:07 2008''

Revision as of 14:13, 20 March 2008

Image:2cay.gif


PDB ID 2cay

Drag the structure with the mouse to rotate
, resolution 1.90Å
Sites:
Ligands:
Coordinates: save as pdb, mmCIF, xml



VPS36 N-TERMINAL PH DOMAIN


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.

About this Structure

2CAY is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

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

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