2ala: Difference between revisions

Line 1:

[[Image:2ala.gif|left|200px]]<br /><applet load="2ala" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:2ala.gif|left|200px]]<br /><applet load="2ala" size="350" color="white" frame="true" align="right" spinBox="true"

caption="2ala, resolution 3.00Å" />

'''Crystal structure of the Semliki Forest Virus envelope protein E1 in its monomeric conformation.'''<br />

==Overview==

Semliki Forest virus (SFV) is enveloped by a lipid bilayer enclosed within, a glycoprotein cage made by glycoproteins E1 and E2. E1 is responsible for, inducing membrane fusion, triggered by exposure to the acidic environment, of the endosomes. Acidic pH induces E1/E2 dissociation, allowing E1 to, interact with the target membrane, and, at the same time, to rearrange, into E1 homotrimers that drive the membrane fusion reaction. We previously, reported a preliminary Calpha trace of the monomeric E1 glycoprotein, ectodomain and its organization on the virus particle. We also reported, the 3.3 A structure of the trimeric, fusogenic conformation of E1. Here, we report the crystal structure of monomeric E1 refined to 3 A resolution, and describe the amino acids involved in contacts in the virion. These, results identify the major determinants for the E1/E2 icosahedral shell, formation and open the way to rational mutagenesis approaches to shed, light on SFV assembly.

Semliki Forest virus (SFV) is enveloped by a lipid bilayer enclosed within a glycoprotein cage made by glycoproteins E1 and E2. E1 is responsible for inducing membrane fusion, triggered by exposure to the acidic environment of the endosomes. Acidic pH induces E1/E2 dissociation, allowing E1 to interact with the target membrane, and, at the same time, to rearrange into E1 homotrimers that drive the membrane fusion reaction. We previously reported a preliminary Calpha trace of the monomeric E1 glycoprotein ectodomain and its organization on the virus particle. We also reported the 3.3 A structure of the trimeric, fusogenic conformation of E1. Here, we report the crystal structure of monomeric E1 refined to 3 A resolution and describe the amino acids involved in contacts in the virion. These results identify the major determinants for the E1/E2 icosahedral shell formation and open the way to rational mutagenesis approaches to shed light on SFV assembly.

==About this Structure==

2ALA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Semliki_forest_virus Semliki forest virus]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2ALA OCA].

2ALA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Semliki_forest_virus Semliki forest virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ALA OCA].

==Reference==

Line 14:

[[Category: Single protein]]

[[Category: Lescar, J.]]

[[Category: Rey, F.A.]]

[[Category: Rey, F A.]]

[[Category: Roussel, A.]]

[[Category: Vaney, M.C.]]

[[Category: Vaney, M C.]]

[[Category: Wengler, G.]]

[[Category: envelope glycoprotein]]

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[[Category: viral protein]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:28:34 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2ala.gif|left|200px]]<br /><applet load="2ala" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2ala.gif|left|200px]]<br /><applet load="2ala" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2ala, resolution 3.00&Aring;" />
 '''Crystal structure of the Semliki Forest Virus envelope protein E1 in its monomeric conformation.'''<br />
 ==Overview==
-Semliki Forest virus (SFV) is enveloped by a lipid bilayer enclosed within, a glycoprotein cage made by glycoproteins E1 and E2. E1 is responsible for, inducing membrane fusion, triggered by exposure to the acidic environment, of the endosomes. Acidic pH induces E1/E2 dissociation, allowing E1 to, interact with the target membrane, and, at the same time, to rearrange, into E1 homotrimers that drive the membrane fusion reaction. We previously, reported a preliminary Calpha trace of the monomeric E1 glycoprotein, ectodomain and its organization on the virus particle. We also reported, the 3.3 A structure of the trimeric, fusogenic conformation of E1. Here, we report the crystal structure of monomeric E1 refined to 3 A resolution, and describe the amino acids involved in contacts in the virion. These, results identify the major determinants for the E1/E2 icosahedral shell, formation and open the way to rational mutagenesis approaches to shed, light on SFV assembly.
+Semliki Forest virus (SFV) is enveloped by a lipid bilayer enclosed within a glycoprotein cage made by glycoproteins E1 and E2. E1 is responsible for inducing membrane fusion, triggered by exposure to the acidic environment of the endosomes. Acidic pH induces E1/E2 dissociation, allowing E1 to interact with the target membrane, and, at the same time, to rearrange into E1 homotrimers that drive the membrane fusion reaction. We previously reported a preliminary Calpha trace of the monomeric E1 glycoprotein ectodomain and its organization on the virus particle. We also reported the 3.3 A structure of the trimeric, fusogenic conformation of E1. Here, we report the crystal structure of monomeric E1 refined to 3 A resolution and describe the amino acids involved in contacts in the virion. These results identify the major determinants for the E1/E2 icosahedral shell formation and open the way to rational mutagenesis approaches to shed light on SFV assembly.
 ==About this Structure==
-ALA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Semliki_forest_virus Semliki forest virus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2ALA OCA].
+ALA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Semliki_forest_virus Semliki forest virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ALA OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Lescar, J.]]
-[[Category: Rey, F.A.]]
+[[Category: Rey, F A.]]
 [[Category: Roussel, A.]]
-[[Category: Vaney, M.C.]]
+[[Category: Vaney, M C.]]
 [[Category: Wengler, G.]]
 [[Category: envelope glycoprotein]]
@@ Line 22: / Line 22: @@
 [[Category: viral protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:12:13 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:28:34 2008''