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5mvf

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Active structure of EHD4 complexed with ADP

Structural highlights

5mvf is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.268Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

EHD4_MOUSE ATP- and membrane-binding protein that probably controls membrane reorganization/tubulation upon ATP hydrolysis. Plays a role in early endosomal transport.^[1]

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Braun A, Pinyol R, Dahlhaus R, Koch D, Fonarev P, Grant BD, Kessels MM, Qualmann B. EHD proteins associate with syndapin I and II and such interactions play a crucial role in endosomal recycling. Mol Biol Cell. 2005 Aug;16(8):3642-58. Epub 2005 Jun 1. PMID:15930129 doi:http://dx.doi.org/10.1091/mbc.E05-01-0076
↑ Melo AA, Hegde BG, Shah C, Larsson E, Isas JM, Kunz S, Lundmark R, Langen R, Daumke O. Structural insights into the activation mechanism of dynamin-like EHD ATPases. Proc Natl Acad Sci U S A. 2017 Feb 22. pii: 201614075. doi:, 10.1073/pnas.1614075114. PMID:28228524 doi:http://dx.doi.org/10.1073/pnas.1614075114

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/5mvf"

Categories: Large Structures | Mus musculus | Daumke O | Melo AA

@@ Line 1: / Line 1: @@
 ==Active structure of EHD4 complexed with ADP==
-<StructureSection load='5mvf' size='340' side='right' caption='[[5mvf]], [[Resolution|resolution]] 3.27&Aring;' scene=''>
+<StructureSection load='5mvf' size='340' side='right'caption='[[5mvf]], [[Resolution|resolution]] 3.27&Aring;' 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>
+<table><tr><td colspan='2'>[[5mvf]] 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=5MVF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.268&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5mtv|5mtv]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5mvf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mvf OCA], [https://pdbe.org/5mvf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mvf RCSB], [https://www.ebi.ac.uk/pdbsum/5mvf PDBsum], [https://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>
+[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 ==
@@ Line 23: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Daumke, O]]
+[[Category: Large Structures]]
-[[Category: Melo, A A]]
+[[Category: Mus musculus]]
-[[Category: Activation]]
+[[Category: Daumke O]]
-[[Category: Auto-inhibition]]
+[[Category: Melo AA]]
-[[Category: Dynamin-like]]
-[[Category: Endocytosis]]

5mvf

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Current revision

Active structure of EHD4 complexed with ADP

Structural highlights

Function

Publication Abstract from PubMed

References

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