1es6

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(New page: 200px<br /><applet load="1es6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1es6, resolution 2.0&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1es6.jpg|left|200px]]<br /><applet load="1es6" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1es6, resolution 2.0&Aring;" />
caption="1es6, resolution 2.0&Aring;" />
'''CRYSTAL STRUCTURE OF THE MATRIX PROTEIN OF EBOLA VIRUS'''<br />
'''CRYSTAL STRUCTURE OF THE MATRIX PROTEIN OF EBOLA VIRUS'''<br />
==Overview==
==Overview==
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Ebola virus maturation occurs at the plasma membrane of infected cells and, involves the clustering of the viral matrix protein VP40 at the assembly, site as well as its interaction with the lipid bilayer. Here we report the, X-ray crystal structure of VP40 from Ebola virus at 2.0 A resolution. The, crystal structure reveals that Ebola virus VP40 is topologically distinct, from all other known viral matrix proteins, consisting of two domains with, unique folds, connected by a flexible linker. The C-terminal domain, which, is absolutely required for membrane binding, contains large hydrophobic, patches that may be involved in the interaction with lipid bilayers., Likewise, a highly basic region is shared between the two domains. The, crystal structure reveals how the molecule may be able to switch from a, monomeric conformation to a hexameric form, as observed in vitro. Its, implications for the assembly process are discussed.
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Ebola virus maturation occurs at the plasma membrane of infected cells and involves the clustering of the viral matrix protein VP40 at the assembly site as well as its interaction with the lipid bilayer. Here we report the X-ray crystal structure of VP40 from Ebola virus at 2.0 A resolution. The crystal structure reveals that Ebola virus VP40 is topologically distinct from all other known viral matrix proteins, consisting of two domains with unique folds, connected by a flexible linker. The C-terminal domain, which is absolutely required for membrane binding, contains large hydrophobic patches that may be involved in the interaction with lipid bilayers. Likewise, a highly basic region is shared between the two domains. The crystal structure reveals how the molecule may be able to switch from a monomeric conformation to a hexameric form, as observed in vitro. Its implications for the assembly process are discussed.
==About this Structure==
==About this Structure==
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1ES6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ebola_virus_sp. Ebola virus sp.]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ES6 OCA].
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1ES6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ebola_virus_sp. Ebola virus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ES6 OCA].
==Reference==
==Reference==
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[[Category: Dessen, A.]]
[[Category: Dessen, A.]]
[[Category: Dolnik, O.]]
[[Category: Dolnik, O.]]
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[[Category: Klenk, H.D.]]
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[[Category: Klenk, H D.]]
[[Category: Volchkov, V.]]
[[Category: Volchkov, V.]]
[[Category: Weissenhorn, W.]]
[[Category: Weissenhorn, W.]]
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[[Category: helix]]
[[Category: helix]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:16:05 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:31:05 2008''

Revision as of 10:31, 21 February 2008


1es6, resolution 2.0Å

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CRYSTAL STRUCTURE OF THE MATRIX PROTEIN OF EBOLA VIRUS

Overview

Ebola virus maturation occurs at the plasma membrane of infected cells and involves the clustering of the viral matrix protein VP40 at the assembly site as well as its interaction with the lipid bilayer. Here we report the X-ray crystal structure of VP40 from Ebola virus at 2.0 A resolution. The crystal structure reveals that Ebola virus VP40 is topologically distinct from all other known viral matrix proteins, consisting of two domains with unique folds, connected by a flexible linker. The C-terminal domain, which is absolutely required for membrane binding, contains large hydrophobic patches that may be involved in the interaction with lipid bilayers. Likewise, a highly basic region is shared between the two domains. The crystal structure reveals how the molecule may be able to switch from a monomeric conformation to a hexameric form, as observed in vitro. Its implications for the assembly process are discussed.

About this Structure

1ES6 is a Single protein structure of sequence from Ebola virus sp.. Full crystallographic information is available from OCA.

Reference

Crystal structure of the matrix protein VP40 from Ebola virus., Dessen A, Volchkov V, Dolnik O, Klenk HD, Weissenhorn W, EMBO J. 2000 Aug 15;19(16):4228-36. PMID:10944105

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