1jmu

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(New page: 200px<br /><applet load="1jmu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jmu, resolution 2.80&Aring;" /> '''Crystal Structure of...)
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[[Image:1jmu.gif|left|200px]]<br /><applet load="1jmu" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1jmu.gif|left|200px]]<br /><applet load="1jmu" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1jmu, resolution 2.80&Aring;" />
caption="1jmu, resolution 2.80&Aring;" />
'''Crystal Structure of the Reovirus mu1/sigma3 Complex'''<br />
'''Crystal Structure of the Reovirus mu1/sigma3 Complex'''<br />
==Overview==
==Overview==
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Cell entry by nonenveloped animal viruses requires membrane penetration, without membrane fusion. The reovirus penetration agent is the, outer-capsid protein, Mu1. The structure of Mu1, complexed with its, "protector" protein, Sigma3, and the fit of this Mu1(3)Sigma3(3), heterohexameric complex into the cryoEM image of an intact virion, reveal, molecular events essential for viral penetration. Autolytic cleavage, divides Mu1 into myristoylated Mu1N and Mu1C. A long hydrophobic pocket, can receive the myristoyl group. Dissociation of Mu1N, linked to a major, conformational change of the entire Mu1 trimer, must precede, myristoyl-group insertion into the cellular membrane. A myristoyl switch, coupling exposure of the fatty acid chain, autolytic cleavage of Mu1N, and, long-range molecular rearrangement of Mu1C, thus appears to be part of the, penetration mechanism.
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Cell entry by nonenveloped animal viruses requires membrane penetration without membrane fusion. The reovirus penetration agent is the outer-capsid protein, Mu1. The structure of Mu1, complexed with its "protector" protein, Sigma3, and the fit of this Mu1(3)Sigma3(3) heterohexameric complex into the cryoEM image of an intact virion, reveal molecular events essential for viral penetration. Autolytic cleavage divides Mu1 into myristoylated Mu1N and Mu1C. A long hydrophobic pocket can receive the myristoyl group. Dissociation of Mu1N, linked to a major conformational change of the entire Mu1 trimer, must precede myristoyl-group insertion into the cellular membrane. A myristoyl switch, coupling exposure of the fatty acid chain, autolytic cleavage of Mu1N, and long-range molecular rearrangement of Mu1C, thus appears to be part of the penetration mechanism.
==About this Structure==
==About this Structure==
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1JMU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Reovirus_sp. Reovirus sp.] with BOG, ZN, SO4, CL and ACE as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JMU OCA].
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1JMU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Reovirus_sp. Reovirus sp.] with <scene name='pdbligand=BOG:'>BOG</scene>, <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JMU OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Reovirus sp.]]
[[Category: Reovirus sp.]]
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[[Category: Harrison, S.C.]]
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[[Category: Harrison, S C.]]
[[Category: Liemann, S.]]
[[Category: Liemann, S.]]
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[[Category: Nibert, M.L.]]
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[[Category: Nibert, M L.]]
[[Category: ACE]]
[[Category: ACE]]
[[Category: BOG]]
[[Category: BOG]]
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[[Category: zinc finger]]
[[Category: zinc finger]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:23:09 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:24:23 2008''

Revision as of 11:24, 21 February 2008

Image:1jmu.gif

1jmu, resolution 2.80Å

Drag the structure with the mouse to rotate

Crystal Structure of the Reovirus mu1/sigma3 Complex

Overview

Cell entry by nonenveloped animal viruses requires membrane penetration without membrane fusion. The reovirus penetration agent is the outer-capsid protein, Mu1. The structure of Mu1, complexed with its "protector" protein, Sigma3, and the fit of this Mu1(3)Sigma3(3) heterohexameric complex into the cryoEM image of an intact virion, reveal molecular events essential for viral penetration. Autolytic cleavage divides Mu1 into myristoylated Mu1N and Mu1C. A long hydrophobic pocket can receive the myristoyl group. Dissociation of Mu1N, linked to a major conformational change of the entire Mu1 trimer, must precede myristoyl-group insertion into the cellular membrane. A myristoyl switch, coupling exposure of the fatty acid chain, autolytic cleavage of Mu1N, and long-range molecular rearrangement of Mu1C, thus appears to be part of the penetration mechanism.

About this Structure

1JMU is a Protein complex structure of sequences from Reovirus sp. with , , , and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of the reovirus membrane-penetration protein, Mu1, in a complex with is protector protein, Sigma3., Liemann S, Chandran K, Baker TS, Nibert ML, Harrison SC, Cell. 2002 Jan 25;108(2):283-95. PMID:11832217

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