4cid

From Proteopedia

(Difference between revisions)

Revision as of 18:05, 4 August 2016

Structural insights into the N-terminus of the EHD2 ATPase

Structural highlights

4cid is a 1 chain structure with sequence from Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
NonStd Res:
Activity:	Dynamin GTPase, with EC number 3.6.5.5
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

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/4cid"

@@ Line 1: / Line 1: @@
 ==Structural insights into the N-terminus of the EHD2 ATPase==
 <StructureSection load='4cid' size='340' side='right' caption='[[4cid]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <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='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://www.rcsb.org/pdb/explore.do?structureId=4cid RCSB], [http://www.ebi.ac.uk/pdbsum/4cid PDBsum]</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>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4cid" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4cid

From Proteopedia

Revision as of 18:05, 4 August 2016

Structural insights into the N-terminus of the EHD2 ATPase

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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