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2qpt

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(New page: 200px<br /><applet load="2qpt" size="350" color="white" frame="true" align="right" spinBox="true" caption="2qpt, resolution 3.10&Aring;" /> '''Crystal structure of...)
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==Overview==
==Overview==
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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. Epsin 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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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==
==About this Structure==
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==Reference==
==Reference==
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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;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17914359 17914359]
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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]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: protein-nucleotide complex]]
[[Category: protein-nucleotide complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:35:06 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:41:23 2008''

Revision as of 16:41, 21 February 2008

Image:2qpt.gif

2qpt, resolution 3.10Å

Drag the structure with the mouse to rotate

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 with , and as ligands. 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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