1hyj

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|PDB= 1hyj |SIZE=350|CAPTION= <scene name='initialview01'>1hyj</scene>
|PDB= 1hyj |SIZE=350|CAPTION= <scene name='initialview01'>1hyj</scene>
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=[[1hyi|1HYI]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hyj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hyj OCA], [http://www.ebi.ac.uk/pdbsum/1hyj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hyj RCSB]</span>
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==Overview==
==Overview==
The recruitment of trafficking and signaling proteins to membranes containing phosphatidylinositol 3-phosphate [PtdIns(3)P] is mediated by FYVE domains. Here, the solution structure of the FYVE domain of the early endosome antigen 1 protein (EEA1) in the free state was compared with the structures of the domain complexed with PtdIns(3)P and mixed micelles. The multistep binding mechanism involved nonspecific insertion of a hydrophobic loop into the lipid bilayer, positioning and activating the binding pocket. Ligation of PtdIns(3)P then induced a global structural change, drawing the protein termini over the bound phosphoinositide by extension of a hinge. Specific recognition of the 3-phosphate was determined indirectly and directly by two clusters of conserved arginines.
The recruitment of trafficking and signaling proteins to membranes containing phosphatidylinositol 3-phosphate [PtdIns(3)P] is mediated by FYVE domains. Here, the solution structure of the FYVE domain of the early endosome antigen 1 protein (EEA1) in the free state was compared with the structures of the domain complexed with PtdIns(3)P and mixed micelles. The multistep binding mechanism involved nonspecific insertion of a hydrophobic loop into the lipid bilayer, positioning and activating the binding pocket. Ligation of PtdIns(3)P then induced a global structural change, drawing the protein termini over the bound phosphoinositide by extension of a hinge. Specific recognition of the 3-phosphate was determined indirectly and directly by two clusters of conserved arginines.
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==Disease==
 
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Known disease associated with this structure: Spastic paraplegia 33 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=610243 610243]]
 
==About this Structure==
==About this Structure==
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[[Category: Kutateladze, T.]]
[[Category: Kutateladze, T.]]
[[Category: Overduin, M.]]
[[Category: Overduin, M.]]
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[[Category: ZN]]
 
[[Category: alpha helix]]
[[Category: alpha helix]]
[[Category: beta sheet]]
[[Category: beta sheet]]
[[Category: zinc cluster]]
[[Category: zinc cluster]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:43:13 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:12:11 2008''

Revision as of 18:12, 30 March 2008


PDB ID 1hyj

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Ligands:
Related: 1HYI


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



SOLUTION STRUCTURE OF THE EEA1 FYVE DOMAIN


Overview

The recruitment of trafficking and signaling proteins to membranes containing phosphatidylinositol 3-phosphate [PtdIns(3)P] is mediated by FYVE domains. Here, the solution structure of the FYVE domain of the early endosome antigen 1 protein (EEA1) in the free state was compared with the structures of the domain complexed with PtdIns(3)P and mixed micelles. The multistep binding mechanism involved nonspecific insertion of a hydrophobic loop into the lipid bilayer, positioning and activating the binding pocket. Ligation of PtdIns(3)P then induced a global structural change, drawing the protein termini over the bound phosphoinositide by extension of a hinge. Specific recognition of the 3-phosphate was determined indirectly and directly by two clusters of conserved arginines.

About this Structure

1HYJ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural mechanism of endosome docking by the FYVE domain., Kutateladze T, Overduin M, Science. 2001 Mar 2;291(5509):1793-6. PMID:11230696

Page seeded by OCA on Sun Mar 30 21:12:11 2008

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