1l9v

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[[Image:1l9v.jpg|left|200px]]
 
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{{Structure
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==Non Structural protein encoded by gene segment 8 of rotavirus (NSP2), an NTPase, ssRNA binding and nucleic acid helix-destabilizing protein==
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|PDB= 1l9v |SIZE=350|CAPTION= <scene name='initialview01'>1l9v</scene>, resolution 2.60&Aring;
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<StructureSection load='1l9v' size='340' side='right'caption='[[1l9v]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1l9v]] is a 1 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)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L9V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L9V FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
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|GENE= gene segment 8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= Simian 11 rotavirus A])
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1l9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l9v OCA], [https://pdbe.org/1l9v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l9v RCSB], [https://www.ebi.ac.uk/pdbsum/1l9v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l9v ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l9v OCA], [http://www.ebi.ac.uk/pdbsum/1l9v PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1l9v RCSB]</span>
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[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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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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'''Non Structural protein encoded by gene segment 8 of rotavirus (NSP2), an NTPase, ssRNA binding and nucleic acid helix-destabilizing protein'''
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l9/1l9v_consurf.spt"</scriptWhenChecked>
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==Overview==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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Rotavirus, the major cause of life-threatening infantile gastroenteritis, is a member of the Reoviridae. Although the structures of rotavirus and other members of the Reoviridae have been extensively studied, little is known about the structures of virus-encoded non-structural proteins that are essential for genome replication and packaging. The non-structural protein NSP2 of rotavirus, which exhibits nucleoside triphosphatase, single-stranded RNA binding, and nucleic-acid helix-destabilizing activities, is a major component of viral replicase complexes. We present here the X-ray structure of the functional octamer of NSP2 determined to a resolution of 2.6 A. The NSP2 monomer has two distinct domains. The amino-terminal domain has a new fold. The carboxy-terminal domain resembles the ubiquitous cellular histidine triad (HIT) group of nucleotidyl hydrolases. This structural similarity suggests that the nucleotide-binding site is located inside the cleft between the two domains. Prominent grooves that run diagonally across the doughnut-shaped octamer are probable locations for RNA binding. Several RNA binding sites, resulting from the quaternary organization of NSP2 monomers, may be required for the helix destabilizing activity of NSP2 and its function during genome replication and packaging.
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==About this Structure==
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</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=1l9v ConSurf].
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1L9V is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Simian_11_rotavirus_a Simian 11 rotavirus a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L9V OCA].
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<div style="clear:both"></div>
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__TOC__
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==Reference==
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</StructureSection>
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Rotavirus protein involved in genome replication and packaging exhibits a HIT-like fold., Jayaram H, Taraporewala Z, Patton JT, Prasad BV, Nature. 2002 May 16;417(6886):311-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12015608 12015608]
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[[Category: Large Structures]]
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[[Category: Simian 11 rotavirus a]]
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[[Category: Jayaram H]]
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[[Category: Single protein]]
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[[Category: Patton JT]]
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[[Category: Jayaram, H.]]
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[[Category: Prasad BV]]
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[[Category: Patton, J T.]]
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[[Category: Taraporewala Z]]
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[[Category: Prasad, B V.]]
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[[Category: Taraporewala, Z.]]
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[[Category: alpha/beta protein]]
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[[Category: hit-like fold]]
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[[Category: octamer]]
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[[Category: two domain protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:00:06 2008''
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Current revision

Non Structural protein encoded by gene segment 8 of rotavirus (NSP2), an NTPase, ssRNA binding and nucleic acid helix-destabilizing protein

PDB ID 1l9v

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