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[[Image:1hyi.jpg|left|200px]]<br /><applet load="1hyi" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1hyi" />
'''SOLUTION STRUCTURE OF THE EEA1 FYVE DOMAIN COMPLEXED WITH INOSITOL 1,3-BISPHOSPHATE'''<br />


==Overview==
==SOLUTION STRUCTURE OF THE EEA1 FYVE DOMAIN COMPLEXED WITH INOSITOL 1,3-BISPHOSPHATE==
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.
<StructureSection load='1hyi' size='340' side='right'caption='[[1hyi]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1hyi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HYI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HYI FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ITP:PHOSPHORIC+ACID+MONO-(2,3,4,6-TETRAHYDROXY-5-PHOSPHONOOXY-CYCLOHEXYL)+ESTER'>ITP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hyi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hyi OCA], [https://pdbe.org/1hyi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hyi RCSB], [https://www.ebi.ac.uk/pdbsum/1hyi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hyi ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/EEA1_HUMAN EEA1_HUMAN] Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate and participates in endosomal trafficking.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hy/1hyi_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1hyi ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Disease==
Structural mechanism of endosome docking by the FYVE domain.,Kutateladze T, Overduin M Science. 2001 Mar 2;291(5509):1793-6. PMID:11230696<ref>PMID:11230696</ref>
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==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1HYI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=ITP:'>ITP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HYI OCA].
</div>
 
<div class="pdbe-citations 1hyi" style="background-color:#fffaf0;"></div>
==Reference==
== References ==
Structural mechanism of endosome docking by the FYVE domain., Kutateladze T, Overduin M, Science. 2001 Mar 2;291(5509):1793-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11230696 11230696]
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Kutateladze, T.]]
[[Category: Kutateladze T]]
[[Category: Overduin, M.]]
[[Category: Overduin M]]
[[Category: ITP]]
[[Category: ZN]]
[[Category: alpha helix]]
[[Category: beta sheet]]
[[Category: ptdins(3)p]]
[[Category: zinc cluster]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:58:42 2008''

Latest revision as of 08:33, 22 May 2024

SOLUTION STRUCTURE OF THE EEA1 FYVE DOMAIN COMPLEXED WITH INOSITOL 1,3-BISPHOSPHATE

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