1uty: Difference between revisions

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New page: left|200px<br /><applet load="1uty" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uty, resolution 2.40Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1uty.gif|left|200px]]<br /><applet load="1uty" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1uty.gif|left|200px]]<br /><applet load="1uty" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1uty, resolution 2.40&Aring;" />
caption="1uty, resolution 2.40&Aring;" />
'''CRYSTAL STRUCTURE OF THE RNA BINDING DOMAIN OF BLUETONGUE VIRUS NON-STRUCTURAL PROTEIN 2(NS2)'''<br />
'''CRYSTAL STRUCTURE OF THE RNA BINDING DOMAIN OF BLUETONGUE VIRUS NON-STRUCTURAL PROTEIN 2(NS2)'''<br />


==Overview==
==Overview==
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.
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 Structure==
==About this Structure==
1UTY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bluetongue_virus Bluetongue virus]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UTY OCA].  
1UTY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bluetongue_virus Bluetongue virus]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UTY OCA].  


==Reference==
==Reference==
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[[Category: Butan, C.]]
[[Category: Butan, C.]]
[[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]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:28:15 2008''

Revision as of 16:28, 21 February 2008

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1uty, resolution 2.40Å

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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. Active as RNA-directed RNA polymerase, with EC number 2.7.7.48 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

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