4g0a: Difference between revisions

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<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='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'>[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://pdbe.org/4g0a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4g0a RCSB], [http://www.ebi.ac.uk/pdbsum/4g0a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4g0a ProSAT]</span></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).
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Rotsr]]
[[Category: Synthetic construct]]
[[Category: Hu, L]]
[[Category: Hu L]]
[[Category: Prasad, B V.V]]
[[Category: Prasad BVV]]
[[Category: Host cell cytoplasm]]
[[Category: Hydrolase activity]]
[[Category: Hydrolase-rna complex]]
[[Category: Metal ion binding]]
[[Category: Nucleotide binding]]
[[Category: Rna binding]]
[[Category: Rna triphosphatase]]

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