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5on7

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Current revision

The ENTH domain from epsin-2 in complex with phosphatidylinositol 4,5-bisphosphate (PIP2)

Structural highlights

5on7 is a 2 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.35Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ENT2_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.^[1]

Publication Abstract from PubMed

In clathrin-mediated endocytosis, adapter proteins assemble together with clathrin through interactions with specific lipids on the plasma membrane. However, the precise mechanism of adapter protein assembly at the cell membrane is still unknown. Here, we show that the membrane-proximal domains ENTH of epsin and ANTH of Sla2 form complexes through phosphatidylinositol 4,5-bisphosphate (PIP2) lipid interfaces. Native mass spectrometry reveals how ENTH and ANTH domains form assemblies by sharing PIP2 molecules. Furthermore, crystal structures of epsin Ent2 ENTH domain from S. cerevisiae in complex with PIP2 and Sla2 ANTH domain from C. thermophilum illustrate how allosteric phospholipid binding occurs. A comparison with human ENTH and ANTH domains reveal only the human ENTH domain can form a stable hexameric core in presence of PIP2, which could explain functional differences between fungal and human epsins. We propose a general phospholipid-driven multifaceted assembly mechanism tolerating different adapter protein compositions to induce endocytosis.

Epsin and Sla2 form assemblies through phospholipid interfaces.,Garcia-Alai MM, Heidemann J, Skruzny M, Gieras A, Mertens HDT, Svergun DI, Kaksonen M, Uetrecht C, Meijers R Nat Commun. 2018 Jan 23;9(1):328. doi: 10.1038/s41467-017-02443-x. PMID:29362354^[2]

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
↑ Garcia-Alai MM, Heidemann J, Skruzny M, Gieras A, Mertens HDT, Svergun DI, Kaksonen M, Uetrecht C, Meijers R. Epsin and Sla2 form assemblies through phospholipid interfaces. Nat Commun. 2018 Jan 23;9(1):328. doi: 10.1038/s41467-017-02443-x. PMID:29362354 doi:http://dx.doi.org/10.1038/s41467-017-02443-x

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5on7"

Categories: Large Structures | Saccharomyces cerevisiae S288C | GIeras A | Garcia-Alai M | Meijers R

@@ Line 3: / Line 3: @@
 <StructureSection load='5on7' size='340' side='right'caption='[[5on7]], [[Resolution|resolution]] 3.35&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5on7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ON7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ON7 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5on7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ON7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ON7 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PIO:[(2R)-2-OCTANOYLOXY-3-[OXIDANYL-[(1R,2R,3S,4R,5R,6S)-2,3,6-TRIS(OXIDANYL)-4,5-DIPHOSPHONOOXY-CYCLOHEXYL]OXY-PHOSPHORYL]OXY-PROPYL]+OCTANOATE'>PIO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.35&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ENT2, YLR206W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PIO:[(2R)-2-OCTANOYLOXY-3-[OXIDANYL-[(1R,2R,3S,4R,5R,6S)-2,3,6-TRIS(OXIDANYL)-4,5-DIPHOSPHONOOXY-CYCLOHEXYL]OXY-PHOSPHORYL]OXY-PROPYL]+OCTANOATE'>PIO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=5on7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5on7 OCA], [http://pdbe.org/5on7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5on7 RCSB], [http://www.ebi.ac.uk/pdbsum/5on7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5on7 ProSAT]</span></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=5on7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5on7 OCA], [https://pdbe.org/5on7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5on7 RCSB], [https://www.ebi.ac.uk/pdbsum/5on7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5on7 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ENT2_YEAST ENT2_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.<ref>PMID:10449404</ref>
+[https://www.uniprot.org/uniprot/ENT2_YEAST ENT2_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.<ref>PMID:10449404</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 19: / Line 19: @@
 </div>
 <div class="pdbe-citations 5on7" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Epsin|Epsin]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Baker's yeast]]
 [[Category: Large Structures]]
-[[Category: GIeras, A]]
+[[Category: Saccharomyces cerevisiae S288C]]
-[[Category: Garcia-Alai, M]]
+[[Category: GIeras A]]
-[[Category: Meijers, R]]
+[[Category: Garcia-Alai M]]
-[[Category: Adaptor protein complex]]
+[[Category: Meijers R]]
-[[Category: Endocytosis]]
-[[Category: Phospholipid binding]]

5on7

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Current revision

The ENTH domain from epsin-2 in complex with phosphatidylinositol 4,5-bisphosphate (PIP2)

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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