1uty: Difference between revisions

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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 2.40Å" />

'''CRYSTAL STRUCTURE OF THE RNA BINDING DOMAIN OF BLUETONGUE VIRUS NON-STRUCTURAL PROTEIN 2(NS2)'''<br />

==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==

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==

Line 16:

[[Category: Butan, C.]]

[[Category: Tucker, P.]]

[[Category: Zandt, H.Van.Der.]]

[[Category: Zandt, H Van Der.]]

[[Category: rna binding protein]]

[[Category: viral protein]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 04:19:~~27 2007~~''

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

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@@ Line 1: / Line 1: @@
-[[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;" />
 '''CRYSTAL STRUCTURE OF THE RNA BINDING DOMAIN OF BLUETONGUE VIRUS NON-STRUCTURAL PROTEIN 2(NS2)'''<br />
 ==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==
-UTY 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].
+UTY 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==
@@ Line 16: / Line 16: @@
 [[Category: Butan, C.]]
 [[Category: Tucker, P.]]
-[[Category: Zandt, H.Van.Der.]]
+[[Category: Zandt, H Van Der.]]
 [[Category: rna binding protein]]
 [[Category: viral protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:19:27 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:28:15 2008''