1uty: Difference between revisions
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< | ==Crystal structure of the RNA binding domain of Bluetongue virus non-structural protein 2(NS2)== | ||
<StructureSection load='1uty' size='340' side='right'caption='[[1uty]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1uty]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bluetongue_virus_8 Bluetongue virus 8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UTY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UTY FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> | |||
-- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1uty FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uty OCA], [https://pdbe.org/1uty PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uty RCSB], [https://www.ebi.ac.uk/pdbsum/1uty PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uty ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/VNS2_BTV10 VNS2_BTV10] Single-stranded RNA-binding protein. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ut/1uty_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1uty ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:15155766</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1uty" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Bluetongue virus 8]] | ||
[[Category: Large Structures]] | |||
[[Category: Butan C]] | |||
== | [[Category: Tucker P]] | ||
< | [[Category: Van Der zandt H]] | ||
[[Category: Bluetongue virus]] | |||
[[Category: | |||
[[Category: Butan | |||
[[Category: Tucker | |||
[[Category: | |||
Latest revision as of 12:05, 9 May 2024
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)
Structural highlights
FunctionVNS2_BTV10 Single-stranded RNA-binding protein. Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedBluetongue 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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