1fn9: Difference between revisions

Revision as of 13:40, 21 February 2008

CRYSTAL STRUCTURE OF THE REOVIRUS OUTER CAPSID PROTEIN SIGMA 3

OverviewOverview

The crystallographically determined structure of the reovirus outer capsid protein sigma3 reveals a two-lobed structure organized around a long central helix. The smaller of the two lobes includes a CCHC zinc-binding site. Residues that vary between strains and serotypes lie mainly on one surface of the protein; residues on the opposite surface are conserved. From a fit of this model to a reconstruction of the whole virion from electron cryomicroscopy, we propose that each sigma3 subunit is positioned with the small lobe anchoring it to the protein mu1 on the surface of the virion, and the large lobe, the site of initial cleavages during entry-related proteolytic disassembly, protruding outwards. The surface containing variable residues faces solvent. The crystallographic asymmetric unit contains two sigma3 subunits, tightly associated as a dimer. One broad surface of the dimer has a positively charged surface patch, which extends across the dyad. In infected cells, sigma3 binds dsRNA and inhibits the interferon response. The location and extent of the positively charged surface patch suggest that the dimer is the RNA-binding form of sigma3.

About this StructureAbout this Structure

1FN9 is a Single protein structure of sequence from Reovirus sp. with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Structure of the reovirus outer capsid and dsRNA-binding protein sigma3 at 1.8 A resolution., Olland AM, Jane-Valbuena J, Schiff LA, Nibert ML, Harrison SC, EMBO J. 2001 Mar 1;20(5):979-89. PMID:11230122

Page seeded by OCA on Thu Feb 21 12:40:28 2008

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OCA

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-[[Image:1fn9.jpg|left|200px]]<br /><applet load="1fn9" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1fn9.jpg|left|200px]]<br /><applet load="1fn9" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1fn9, resolution 1.8&Aring;" />
 '''CRYSTAL STRUCTURE OF THE REOVIRUS OUTER CAPSID PROTEIN SIGMA 3'''<br />
 ==Overview==
-The crystallographically determined structure of the reovirus outer capsid, protein sigma3 reveals a two-lobed structure organized around a long, central helix. The smaller of the two lobes includes a CCHC zinc-binding, site. Residues that vary between strains and serotypes lie mainly on one, surface of the protein; residues on the opposite surface are conserved., From a fit of this model to a reconstruction of the whole virion from, electron cryomicroscopy, we propose that each sigma3 subunit is positioned, with the small lobe anchoring it to the protein mu1 on the surface of the, virion, and the large lobe, the site of initial cleavages during, entry-related proteolytic disassembly, protruding outwards. The surface, containing variable residues faces solvent. The crystallographic, asymmetric unit contains two sigma3 subunits, tightly associated as a, dimer. One broad surface of the dimer has a positively charged surface, patch, which extends across the dyad. In infected cells, sigma3 binds, dsRNA and inhibits the interferon response. The location and extent of the, positively charged surface patch suggest that the dimer is the RNA-binding, form of sigma3.
+The crystallographically determined structure of the reovirus outer capsid protein sigma3 reveals a two-lobed structure organized around a long central helix. The smaller of the two lobes includes a CCHC zinc-binding site. Residues that vary between strains and serotypes lie mainly on one surface of the protein; residues on the opposite surface are conserved. From a fit of this model to a reconstruction of the whole virion from electron cryomicroscopy, we propose that each sigma3 subunit is positioned with the small lobe anchoring it to the protein mu1 on the surface of the virion, and the large lobe, the site of initial cleavages during entry-related proteolytic disassembly, protruding outwards. The surface containing variable residues faces solvent. The crystallographic asymmetric unit contains two sigma3 subunits, tightly associated as a dimer. One broad surface of the dimer has a positively charged surface patch, which extends across the dyad. In infected cells, sigma3 binds dsRNA and inhibits the interferon response. The location and extent of the positively charged surface patch suggest that the dimer is the RNA-binding form of sigma3.
 ==About this Structure==
-FN9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Reovirus_sp. Reovirus sp.] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FN9 OCA].
+FN9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Reovirus_sp. Reovirus sp.] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FN9 OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Reovirus sp.]]
 [[Category: Single protein]]
-[[Category: Harrison, S.C.]]
+[[Category: Harrison, S C.]]
 [[Category: Jane-Valbuena, J.]]
-[[Category: Nibert, M.L.]]
+[[Category: Nibert, M L.]]
-[[Category: Olland, A.M.]]
+[[Category: Olland, A M.]]
-[[Category: Schiff, L.A.]]
+[[Category: Schiff, L A.]]
 [[Category: ZN]]
 [[Category: zinc binding motif]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 00:06:09 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:40:28 2008''