5loz

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m (Protected "5loz" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5loz is ON HOLD until Paper Publication
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==STRUCTURE OF YEAST ENT1 ENTH DOMAIN==
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<StructureSection load='5loz' size='340' side='right' caption='[[5loz]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5loz]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LOZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LOZ FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1hoa|1hoa]], [[1edu|1edu]], [[1eyh|1eyh]]</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5loz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5loz OCA], [http://pdbe.org/5loz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5loz RCSB], [http://www.ebi.ac.uk/pdbsum/5loz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5loz ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/ENT1_YEAST ENT1_YEAST]] Binds to membranes enriched in phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) and phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Required for endocytosis and localization of actin. Negatively regulated via phosphorylation.<ref>PMID:10449404</ref> <ref>PMID:11694597</ref> <ref>PMID:12529323</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Members of the Epsin protein family regulate the ubiquitin/clathrin-dependent trafficking of transmembrane proteins. The yeast Epsin-1 (ent1) gene was cloned and expressed in Escherichia coli. The protein product of a construct containing the ENTH-UIM modules was purified to homogeneity and subjected to crystallization screening using the sitting-drop vapour-diffusion method. Refined conditions containing polyethylene glycol 3350 and Tacsimate yielded thin rod-like crystals. X-ray analysis revealed that the crystallographic symmetry is primitive orthorhombic, space group P222, with unit-cell parameters a = 32.7, b = 35.5, c = 110.6 A and a diffraction limit of 2.3 A. Matthews coefficient calculations suggested that the crystal contained only the ENTH domain. This was corroborated by Coomassie Blue-stained SDS-PAGE analysis of dissolved crystals.
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Authors: Tanner, N., Prag, G.
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Purification and crystallization of yeast Ent1 ENTH domain.,Tanner N, Prag G Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Jul 1;68(Pt 7):820-3. doi:, 10.1107/S1744309112022488. Epub 2012 Jun 28. PMID:22750874<ref>PMID:22750874</ref>
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Description: STRUCTURE OF YEAST ENT1 ENTH DOMAIN
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5loz" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Prag, G]]
[[Category: Prag, G]]
[[Category: Tanner, N]]
[[Category: Tanner, N]]
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[[Category: Alpha-alpha superhelix]]
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[[Category: Clathrin]]
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[[Category: Endocytosis adaptor]]
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[[Category: Eps15]]
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[[Category: Lipid]]
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[[Category: Ubiquitin]]
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[[Category: Ubiquitin receptor]]
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[[Category: Ubiquitin-binding domain]]

Revision as of 21:39, 5 October 2016

STRUCTURE OF YEAST ENT1 ENTH DOMAIN

5loz, resolution 1.95Å

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