This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

5onf

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

The ENTH domain from epsin-1

Structural highlights

5onf is a 3 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 2.8Å
Ligands:
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

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^[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
↑ 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/5onf"

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

@@ Line 1: / Line 1: @@
 ==The ENTH domain from epsin-1==
-<StructureSection load='5onf' size='340' side='right' caption='[[5onf]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
+<StructureSection load='5onf' size='340' side='right'caption='[[5onf]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5onf]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ONF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ONF FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5onf]] is a 3 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=5ONF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ONF FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</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]] 2.8&#8491;</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=5onf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5onf OCA], [http://pdbe.org/5onf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5onf RCSB], [http://www.ebi.ac.uk/pdbsum/5onf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5onf ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</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=5onf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5onf OCA], [https://pdbe.org/5onf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5onf RCSB], [https://www.ebi.ac.uk/pdbsum/5onf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5onf 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>
+[https://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 ==
@@ Line 18: / Line 19: @@
 </div>
 <div class="pdbe-citations 5onf" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Epsin|Epsin]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: GIeras, A]]
+[[Category: Large Structures]]
-[[Category: Garcia-Alai, M]]
+[[Category: Saccharomyces cerevisiae S288C]]
-[[Category: Meijers, R]]
+[[Category: GIeras A]]
-[[Category: Adaptor protein complex]]
+[[Category: Garcia-Alai M]]
-[[Category: Endocytosis]]
+[[Category: Meijers R]]

5onf

From Proteopedia

Current revision

The ENTH domain from epsin-1

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox