2qpt
From Proteopedia
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|PDB= 2qpt |SIZE=350|CAPTION= <scene name='initialview01'>2qpt</scene>, resolution 3.10Å | |PDB= 2qpt |SIZE=350|CAPTION= <scene name='initialview01'>2qpt</scene>, resolution 3.10Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <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> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= Ehd2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | |GENE= Ehd2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qpt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qpt OCA], [http://www.ebi.ac.uk/pdbsum/2qpt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2qpt RCSB]</span> | ||
}} | }} | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Daumke, O.]] | [[Category: Daumke, O.]] | ||
| - | [[Category: ANP]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: MG]] | ||
[[Category: endocytosis]] | [[Category: endocytosis]] | ||
[[Category: membrane protein]] | [[Category: membrane protein]] | ||
[[Category: protein-nucleotide complex]] | [[Category: protein-nucleotide complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:51:58 2008'' |
Revision as of 01:51, 31 March 2008
| |||||||
| , resolution 3.10Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | Ehd2 (Mus musculus) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of an EHD ATPase involved in membrane remodelling
Overview
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.
About this Structure
2QPT is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
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:17914359
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