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2qpt

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[[Image:2qpt.gif|left|200px]]<br /><applet load="2qpt" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2qpt, resolution 3.10&Aring;" />
 
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'''Crystal structure of an EHD ATPase involved in membrane remodelling'''<br />
 
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==Overview==
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==Crystal structure of an EHD ATPase involved in membrane remodelling==
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The ability to actively remodel membranes in response to nucleotide hydrolysis has largely been attributed to GTPases of the dynamin superfamily, and these have been extensively studied. Eps15 homology (EH)-domain-containing proteins (EHDs/RME-1/pincher) comprise a less-well-characterized class of highly conserved eukaryotic ATPases implicated in clathrin-independent endocytosis, and recycling from endosomes. Here we show that EHDs share many common features with the dynamin superfamily, such as a low affinity for nucleotides, the ability to tubulate liposomes in vitro, oligomerization around lipid tubules in ring-like structures and stimulated nucleotide hydrolysis in response to lipid binding. We present the structure of EHD2, bound to a non-hydrolysable ATP analogue, and provide evidence consistent with a role for EHDs in nucleotide-dependent membrane remodelling in vivo. The nucleotide-binding domain is involved in dimerization, which creates a highly curved membrane-binding region in the dimer. Oligomerization of dimers occurs on another interface of the nucleotide-binding domain, and this allows us to model the EHD oligomer. We discuss the functional implications of the EHD2 structure for understanding membrane deformation.
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<StructureSection load='2qpt' size='340' side='right'caption='[[2qpt]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[2qpt]] 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=2QPT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QPT FirstGlance]. <br>
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2QPT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=ANP:'>ANP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QPT OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
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<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></td></tr>
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==Reference==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qpt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qpt OCA], [https://pdbe.org/2qpt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qpt RCSB], [https://www.ebi.ac.uk/pdbsum/2qpt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qpt ProSAT]</span></td></tr>
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Architectural and mechanistic insights into an EHD ATPase involved in membrane remodelling., Daumke O, Lundmark R, Vallis Y, Martens S, Butler PJ, McMahon HT, Nature. 2007 Oct 3;449(7164):923-927. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17914359 17914359]
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qp/2qpt_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2qpt ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Single protein]]
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[[Category: Daumke O]]
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[[Category: Daumke, O.]]
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[[Category: ANP]]
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[[Category: CA]]
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[[Category: MG]]
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[[Category: endocytosis]]
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[[Category: membrane protein]]
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[[Category: protein-nucleotide complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:41:23 2008''
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Current revision

Crystal structure of an EHD ATPase involved in membrane remodelling

PDB ID 2qpt

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