7sox
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7sox]] is a 16 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=7SOX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SOX FirstGlance]. <br> | <table><tr><td colspan='2'>[[7sox]] is a 16 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=7SOX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SOX FirstGlance]. <br> | ||
| - | </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=7sox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7sox OCA], [https://pdbe.org/7sox PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7sox RCSB], [https://www.ebi.ac.uk/pdbsum/7sox PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7sox ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 7.6Å</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=7sox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7sox OCA], [https://pdbe.org/7sox PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7sox RCSB], [https://www.ebi.ac.uk/pdbsum/7sox PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7sox ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/EHD4_MOUSE EHD4_MOUSE] ATP- and membrane-binding protein that probably controls membrane reorganization/tubulation upon ATP hydrolysis. Plays a role in early endosomal transport.<ref>PMID:15930129</ref> | [https://www.uniprot.org/uniprot/EHD4_MOUSE EHD4_MOUSE] ATP- and membrane-binding protein that probably controls membrane reorganization/tubulation upon ATP hydrolysis. Plays a role in early endosomal transport.<ref>PMID:15930129</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Eps15-homology domain containing proteins (EHDs) are eukaryotic, dynamin-related ATPases involved in cellular membrane trafficking. They oligomerize on membranes into filaments that induce membrane tubulation. While EHD crystal structures in open and closed conformations were previously reported, little structural information is available for the membrane-bound oligomeric form. Consequently, mechanistic insights into the membrane remodeling mechanism have remained sparse. Here, by using cryo-electron tomography and subtomogram averaging, we determined structures of nucleotide-bound EHD4 filaments on membrane tubes of various diameters at an average resolution of 7.6 A. Assembly of EHD4 is mediated via interfaces in the G-domain and the helical domain. The oligomerized EHD4 structure resembles the closed conformation, where the tips of the helical domains protrude into the membrane. The variation in filament geometry and tube radius suggests a spontaneous filament curvature of approximately 1/70 nm(-1). Combining the available structural and functional data, we suggest a model for EHD-mediated membrane remodeling. | ||
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| + | Cryo-electron tomography reveals structural insights into the membrane remodeling mode of dynamin-like EHD filaments.,Melo AA, Sprink T, Noel JK, Vazquez-Sarandeses E, van Hoorn C, Mohd S, Loerke J, Spahn CMT, Daumke O Nat Commun. 2022 Dec 10;13(1):7641. doi: 10.1038/s41467-022-35164-x. PMID:36496453<ref>PMID:36496453</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7sox" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Cryo-electron tomography structure of membrane-bound EHD4 complex
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