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==Crystallographic Analysis of Rotavirus NSP2-RNA Complex Reveals Specific Recognition of 5'-GG Sequence for RTPase activity==
==Crystallographic Analysis of Rotavirus NSP2-RNA Complex Reveals Specific Recognition of 5'-GG Sequence for RTPase activity==
<StructureSection load='4g0a' size='340' side='right' caption='[[4g0a]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='4g0a' size='340' side='right'caption='[[4g0a]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4g0a]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Rotsr Rotsr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G0A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G0A FirstGlance]. <br>
<table><tr><td colspan='2'>[[4g0a]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Simian_11_rotavirus_(serotype_3_/_strain_SA11-Ramig) Simian 11 rotavirus (serotype 3 / strain SA11-Ramig)] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G0A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G0A FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.0995&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4g0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g0a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4g0a RCSB], [http://www.ebi.ac.uk/pdbsum/4g0a PDBsum]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=4g0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g0a OCA], [https://pdbe.org/4g0a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g0a RCSB], [https://www.ebi.ac.uk/pdbsum/4g0a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g0a ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/NSP2_ROTSR NSP2_ROTSR]] Involved in genome replication and packaging. Plays a crucial role, together with NSP5, in the formation of virus factories (viroplasms) which are large inclusions in the cytoplasm where replication intermediates are assembled and RNA replication takes place. Displays ssRNA binding, NTPase, RNA triphosphatase (RTPase) and ATP-independent helix-unwinding activity activities. The unwiding activity may prepare and organize plus-strand RNAs for packaging and replication by removing interfering secondary structures. Unlike typical helicases, NSP2 requires neither a divalent cation nor a nucleotide energy source for helix destabilization. The RTPase activity may account for the absence of the 5'-terminal gamma-phosphate on the minus-strands of dsRNA genome segments (By similarity).  
[https://www.uniprot.org/uniprot/NSP2_ROTSR NSP2_ROTSR] Involved in genome replication and packaging. Plays a crucial role, together with NSP5, in the formation of virus factories (viroplasms) which are large inclusions in the cytoplasm where replication intermediates are assembled and RNA replication takes place. Displays ssRNA binding, NTPase, RNA triphosphatase (RTPase) and ATP-independent helix-unwinding activity activities. The unwiding activity may prepare and organize plus-strand RNAs for packaging and replication by removing interfering secondary structures. Unlike typical helicases, NSP2 requires neither a divalent cation nor a nucleotide energy source for helix destabilization. The RTPase activity may account for the absence of the 5'-terminal gamma-phosphate on the minus-strands of dsRNA genome segments (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Rotavirus non-structural protein NSP2, a functional octamer, is critical for the formation of viroplasms, which are exclusive sites for replication and packaging of segmented double-stranded RNA (dsRNA) rotavirus genome. As a component of replication intermediates, NSP2 is also implicated in various replication-related activities. In addition to sequence-independent single-stranded RNA binding and helix-destabilizing activities, NSP2 exhibits monomer-associated nucleoside and 5' RNA triphosphatase (NTPase/RTPase) activities which are mediated by a conserved H225 residue within a narrow enzymatic cleft. Lack of a 5' gamma-phosphate is a common feature of the (-)RNA of the packaged dsRNA segments in RV. Strikingly, all (-)RNAs (in group A RV) have a 5' GG dinucleotide sequence. As the only rotavirus protein with 5' RTPase activity, NSP2 is implicated in the removal of the gamma-phosphate from the rotavirus minus-strand RNA. To understand how NSP2, despite its sequence-independent RNA binding property, recognizes minus-strand RNA to hydrolyze the gamma-phosphate within the catalytic cleft, we determined a crystal structure of NSP2 in complex with the 5' consensus sequence of minus-strand rotavirus RNA. Our studies show that the 5' GG of the bound oligoribonucleotide interacts extensively with highly conserved residues in the NSP2 enzymatic cleft. While these residues provide GG-specific interactions, surface plasmon resonance studies suggest that the C-terminal helix and other basic residues outside the enzymatic cleft account for sequence-independent RNA binding of NSP2. A novel observation from our studies, which may have implications in viroplasm formation, is that the C-terminal helix of NSP2 exhibits two distinct conformations and engages in domain swapping interactions, which result in the formation of NSP2 octamer chains.
 
Crystallographic Analysis of Rotavirus NSP2-RNA Complex Reveals Specific Recognition of 5' -GG Sequence for RTPase activity.,Hu L, Chow DC, Patton JT, Palzkill T, Estes MK, Prasad BV J Virol. 2012 Jul 18. PMID:22811529<ref>PMID:22811529</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Rotsr]]
[[Category: Large Structures]]
[[Category: Hu, L]]
[[Category: Synthetic construct]]
[[Category: Prasad, B V.V]]
[[Category: Hu L]]
[[Category: Host cell cytoplasm]]
[[Category: Prasad BVV]]
[[Category: Hydrolase activity]]
[[Category: Hydrolase-rna complex]]
[[Category: Metal ion binding]]
[[Category: Nucleotide binding]]
[[Category: Rna binding]]
[[Category: Rna triphosphatase]]

Latest revision as of 14:24, 1 March 2024

Crystallographic Analysis of Rotavirus NSP2-RNA Complex Reveals Specific Recognition of 5'-GG Sequence for RTPase activityCrystallographic Analysis of Rotavirus NSP2-RNA Complex Reveals Specific Recognition of 5'-GG Sequence for RTPase activity

Structural highlights

4g0a is a 8 chain structure with sequence from Simian 11 rotavirus (serotype 3 / strain SA11-Ramig) and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.0995Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NSP2_ROTSR Involved in genome replication and packaging. Plays a crucial role, together with NSP5, in the formation of virus factories (viroplasms) which are large inclusions in the cytoplasm where replication intermediates are assembled and RNA replication takes place. Displays ssRNA binding, NTPase, RNA triphosphatase (RTPase) and ATP-independent helix-unwinding activity activities. The unwiding activity may prepare and organize plus-strand RNAs for packaging and replication by removing interfering secondary structures. Unlike typical helicases, NSP2 requires neither a divalent cation nor a nucleotide energy source for helix destabilization. The RTPase activity may account for the absence of the 5'-terminal gamma-phosphate on the minus-strands of dsRNA genome segments (By similarity).

4g0a, resolution 2.10Å

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