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| | <StructureSection load='4cid' size='340' side='right'caption='[[4cid]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='4cid' size='340' side='right'caption='[[4cid]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4cid]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CID OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CID FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4cid]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CID OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CID FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=4cid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cid OCA], [https://pdbe.org/4cid PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cid RCSB], [https://www.ebi.ac.uk/pdbsum/4cid PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cid ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dynamin_GTPase Dynamin GTPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.5.5 3.6.5.5] </span></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=4cid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cid OCA], [http://pdbe.org/4cid PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cid RCSB], [http://www.ebi.ac.uk/pdbsum/4cid PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cid ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/EHD2_MOUSE EHD2_MOUSE]] Plays a role in membrane reorganization in response to nucleotide hydrolysis. Binds to liposomes and deforms them into tubules. Plays a role in membrane trafficking between the plasma membrane and endosomes. Important for the internalization of GLUT4. Required for normal fusion of myoblasts to skeletal muscle myotubes. Binds ATP; does not bind GTP.<ref>PMID:14676205</ref> <ref>PMID:18502764</ref> | + | [[https://www.uniprot.org/uniprot/EHD2_MOUSE EHD2_MOUSE]] Plays a role in membrane reorganization in response to nucleotide hydrolysis. Binds to liposomes and deforms them into tubules. Plays a role in membrane trafficking between the plasma membrane and endosomes. Important for the internalization of GLUT4. Required for normal fusion of myoblasts to skeletal muscle myotubes. Binds ATP; does not bind GTP.<ref>PMID:14676205</ref> <ref>PMID:18502764</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Dynamin GTPase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Daumke, O]] | + | [[Category: Daumke O]] |
| - | [[Category: Shah, C]] | + | [[Category: Shah C]] |
| - | [[Category: Dynamin superfamily]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Mechanochemical atpase]]
| + | |
| Structural highlights
Function
[EHD2_MOUSE] Plays a role in membrane reorganization in response to nucleotide hydrolysis. Binds to liposomes and deforms them into tubules. Plays a role in membrane trafficking between the plasma membrane and endosomes. Important for the internalization of GLUT4. Required for normal fusion of myoblasts to skeletal muscle myotubes. Binds ATP; does not bind GTP.[1] [2]
Publication Abstract from PubMed
The dynamin-related Eps15-homology domain-containing protein 2 (EHD2) is a membrane-remodeling ATPase that regulates the dynamics of caveolae. Here, we established an electron paramagnetic resonance (EPR) approach to characterize structural features of membrane-bound EHD2. We show that residues at the tip of the helical domain can insert into the membrane and may create membrane curvature by a wedging mechanism. Using EPR and X-ray crystallography, we found that the N terminus is folded into a hydrophobic pocket of the GTPase domain in solution and can be released into the membrane. Cryoelectron microscopy demonstrated that the N terminus is not essential for oligomerization of EHD2 into a membrane-anchored scaffold. Instead, we found a function of the N terminus in regulating targeting and stable association of EHD2 to caveolae. Our data uncover an unexpected, membrane-induced regulatory switch in EHD2 and demonstrate the versatility of EPR to study structure and function of dynamin superfamily proteins.
Structural Insights into Membrane Interaction and Caveolar Targeting of Dynamin-like EHD2.,Shah C, Hegde BG, Moren B, Behrmann E, Mielke T, Moenke G, Spahn CM, Lundmark R, Daumke O, Langen R Structure. 2014 Feb 4. pii: S0969-2126(14)00007-0. doi:, 10.1016/j.str.2013.12.015. PMID:24508342[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Guilherme A, Soriano NA, Bose S, Holik J, Bose A, Pomerleau DP, Furcinitti P, Leszyk J, Corvera S, Czech MP. EHD2 and the novel EH domain binding protein EHBP1 couple endocytosis to the actin cytoskeleton. J Biol Chem. 2004 Mar 12;279(11):10593-605. Epub 2003 Dec 15. PMID:14676205 doi:http://dx.doi.org/10.1074/jbc.M307702200
- ↑ Doherty KR, Demonbreun AR, Wallace GQ, Cave A, Posey AD, Heretis K, Pytel P, McNally EM. The endocytic recycling protein EHD2 interacts with myoferlin to regulate myoblast fusion. J Biol Chem. 2008 Jul 18;283(29):20252-60. Epub 2008 May 23. PMID:18502764 doi:http://dx.doi.org/M802306200
- ↑ Shah C, Hegde BG, Moren B, Behrmann E, Mielke T, Moenke G, Spahn CM, Lundmark R, Daumke O, Langen R. Structural Insights into Membrane Interaction and Caveolar Targeting of Dynamin-like EHD2. Structure. 2014 Feb 4. pii: S0969-2126(14)00007-0. doi:, 10.1016/j.str.2013.12.015. PMID:24508342 doi:http://dx.doi.org/10.1016/j.str.2013.12.015
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