5mvf
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Active structure of EHD4 complexed with ADP== | |
| + | <StructureSection load='5mvf' size='340' side='right' caption='[[5mvf]], [[Resolution|resolution]] 3.27Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5mvf]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MVF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MVF FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5mtv|5mtv]]</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=5mvf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mvf OCA], [http://pdbe.org/5mvf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mvf RCSB], [http://www.ebi.ac.uk/pdbsum/5mvf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mvf ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://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 (epidermal growth factor receptor pathway substrate 15)-homology domain containing proteins (EHDs) comprise a family of dynamin-related mechano-chemical ATPases involved in cellular membrane trafficking. Previous studies have revealed the structure of the EHD2 dimer, but the molecular mechanisms of membrane recruitment and assembly have remained obscure. Here, we determined the crystal structure of an amino-terminally truncated EHD4 dimer. Compared with the EHD2 structure, the helical domains are 50 degrees rotated relative to the GTPase domain. Using electron paramagnetic spin resonance (EPR), we show that this rotation aligns the two membrane-binding regions in the helical domain toward the lipid bilayer, allowing membrane interaction. A loop rearrangement in GTPase domain creates a new interface for oligomer formation. Our results suggest that the EHD4 structure represents the active EHD conformation, whereas the EHD2 structure is autoinhibited, and reveal a complex series of domain rearrangements accompanying activation. A comparison with other peripheral membrane proteins elucidates common and specific features of this activation mechanism. | ||
| - | + | Structural insights into the activation mechanism of dynamin-like EHD ATPases.,Melo AA, Hegde BG, Shah C, Larsson E, Isas JM, Kunz S, Lundmark R, Langen R, Daumke O Proc Natl Acad Sci U S A. 2017 Feb 22. pii: 201614075. doi:, 10.1073/pnas.1614075114. PMID:28228524<ref>PMID:28228524</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5mvf" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Daumke, O]] | [[Category: Daumke, O]] | ||
| + | [[Category: Melo, A A]] | ||
| + | [[Category: Activation]] | ||
| + | [[Category: Auto-inhibition]] | ||
| + | [[Category: Dynamin-like]] | ||
| + | [[Category: Endocytosis]] | ||
Revision as of 16:50, 9 March 2017
Active structure of EHD4 complexed with ADP
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