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5loz

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Revision as of 21:39, 5 October 2016

STRUCTURE OF YEAST ENT1 ENTH DOMAIN

Structural highlights

5loz is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1hoa, 1edu, 1eyh
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2] ^[3]

Publication Abstract from PubMed

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.

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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Wendland B, Steece KE, Emr SD. Yeast epsins contain an essential N-terminal ENTH domain, bind clathrin and are required for endocytosis. EMBO J. 1999 Aug 16;18(16):4383-93. PMID:10449404 doi:10.1093/emboj/18.16.4383
↑ Watson HA, Cope MJ, Groen AC, Drubin DG, Wendland B. In vivo role for actin-regulating kinases in endocytosis and yeast epsin phosphorylation. Mol Biol Cell. 2001 Nov;12(11):3668-79. PMID:11694597
↑ Aguilar RC, Watson HA, Wendland B. The yeast Epsin Ent1 is recruited to membranes through multiple independent interactions. J Biol Chem. 2003 Mar 21;278(12):10737-43. Epub 2003 Jan 14. PMID:12529323 doi:http://dx.doi.org/10.1074/jbc.M211622200
↑ Unknown PubmedID 22750874

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5loz"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5loz is ON HOLD  until Paper Publication
+==STRUCTURE OF YEAST ENT1 ENTH DOMAIN==
+<StructureSection load='5loz' size='340' side='right' caption='[[5loz]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
+== Structural highlights ==
+<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>
+</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>
+<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>
+</table>
+== Function ==
+[[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>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-Authors: Tanner, N., Prag, G.
+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>
-Description: STRUCTURE OF YEAST ENT1 ENTH DOMAIN
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5loz" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Prag, G]]
 [[Category: Tanner, N]]
+[[Category: Alpha-alpha superhelix]]
+[[Category: Clathrin]]
+[[Category: Endocytosis adaptor]]
+[[Category: Eps15]]
+[[Category: Lipid]]
+[[Category: Ubiquitin]]
+[[Category: Ubiquitin receptor]]
+[[Category: Ubiquitin-binding domain]]

5loz

From Proteopedia

Revision as of 21:39, 5 October 2016

STRUCTURE OF YEAST ENT1 ENTH DOMAIN

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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