1uty: Difference between revisions

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[[Image:1uty.gif|left|200px]]
[[Image:1uty.gif|left|200px]]


{{Structure
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/RNA-directed_RNA_polymerase RNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.48 2.7.7.48] </span>
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'''CRYSTAL STRUCTURE OF THE RNA BINDING DOMAIN OF BLUETONGUE VIRUS NON-STRUCTURAL PROTEIN 2(NS2)'''
'''CRYSTAL STRUCTURE OF THE RNA BINDING DOMAIN OF BLUETONGUE VIRUS NON-STRUCTURAL PROTEIN 2(NS2)'''
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[[Category: Tucker, P.]]
[[Category: Tucker, P.]]
[[Category: Zandt, H Van Der.]]
[[Category: Zandt, H Van Der.]]
[[Category: rna binding protein]]
[[Category: Rna binding protein]]
[[Category: viral protein]]
[[Category: Viral protein]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 11:41:08 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:15:12 2008''

Revision as of 11:41, 3 May 2008

File:1uty.gif

Template:STRUCTURE 1uty

CRYSTAL STRUCTURE OF THE RNA BINDING DOMAIN OF BLUETONGUE VIRUS NON-STRUCTURAL PROTEIN 2(NS2)


OverviewOverview

Bluetongue virus non-structural protein 2 belongs to a class of highly conserved proteins found in orbiviruses of the Reoviridae family. Non-structural protein 2 forms large multimeric complexes and localizes to cytoplasmic inclusions in infected cells. It is able to bind single-stranded RNA non-specifically, and it has been suggested that the protein is involved in the selection and condensation of the Bluetongue virus RNA segments prior to genome encapsidation. We have determined the x-ray structure of the N-terminal domain (sufficient for the RNA binding ability of non-structural protein 2) to 2.4 A resolution using anomalous scattering methods. Crystals of this apparently insoluble domain were obtained by in situ proteolysis of a soluble construct. The asymmetric unit shows two monomers related by non-crystallographic symmetry, with each monomer folded as a beta sandwich with a unique topology. The crystal structure reveals extensive monomer-monomer interactions, which explain the ability of the protein to self-assemble into large homomultimeric complexes. Of the entire surface area of the monomer, one-third is used to create the interfaces of the curved multimeric assembly observed in the x-ray structure. The structure reported here shows how the N-terminal domain would be able to bind single-stranded RNA non-specifically protecting the bound regions in a heterogeneous multimeric but not polymeric complex.

About this StructureAbout this Structure

1UTY is a Single protein structure of sequence from Bluetongue virus. Full crystallographic information is available from OCA.

ReferenceReference

Structure and assembly of the RNA binding domain of bluetongue virus non-structural protein 2., Butan C, Van Der Zandt H, Tucker PA, J Biol Chem. 2004 Sep 3;279(36):37613-21. Epub 2004 May 20. PMID:15155766 Page seeded by OCA on Sat May 3 11:41:08 2008

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