1fn9: Difference between revisions

Revision as of 03:36, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1fn9.png

Template:STRUCTURE 1fn9

CRYSTAL STRUCTURE OF THE REOVIRUS OUTER CAPSID PROTEIN SIGMA 3CRYSTAL STRUCTURE OF THE REOVIRUS OUTER CAPSID PROTEIN SIGMA 3

Template:ABSTRACT PUBMED 11230122

About this StructureAbout this Structure

1FN9 is a Single protein structure of sequence from Reovirus sp.. 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

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OCA

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-'''CRYSTAL STRUCTURE OF THE REOVIRUS OUTER CAPSID PROTEIN SIGMA 3'''
+===CRYSTAL STRUCTURE OF THE REOVIRUS OUTER CAPSID PROTEIN SIGMA 3===
-==Overview==
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-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 line below this paragraph, {{ABSTRACT_PUBMED_11230122}}, adds the Publication Abstract to the page
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 ==About this Structure==
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 [[Category: Schiff, L A.]]
 [[Category: Zinc binding motif]]
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