1n38

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<StructureSection load='1n38' size='340' side='right'caption='[[1n38]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='1n38' size='340' side='right'caption='[[1n38]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1n38]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Mammalian_orthoreovirus_3_strain_dearing Mammalian orthoreovirus 3 strain dearing]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N38 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1N38 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1n38]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mammalian_orthoreovirus_3_Dearing Mammalian orthoreovirus 3 Dearing]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N38 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N38 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CH1:3-DEOXY-CYTIDINE-5-TRIPHOSPHATE'>CH1</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=U3H:3-DEOXY-URIDINE+5-TRIPHOSPHATE'>U3H</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CH1:3-DEOXY-CYTIDINE-5-TRIPHOSPHATE'>CH1</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=U3H:3-DEOXY-URIDINE+5-TRIPHOSPHATE'>U3H</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1muk|1muk]], [[1mwh|1mwh]], [[1n1h|1n1h]], [[1n35|1n35]]</div></td></tr>
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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=1n38 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n38 OCA], [https://pdbe.org/1n38 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n38 RCSB], [https://www.ebi.ac.uk/pdbsum/1n38 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n38 ProSAT]</span></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">L1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10886 Mammalian Orthoreovirus 3 strain Dearing])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1n38 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n38 OCA], [http://pdbe.org/1n38 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1n38 RCSB], [http://www.ebi.ac.uk/pdbsum/1n38 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1n38 ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[[https://www.uniprot.org/uniprot/RDRP_REOVD RDRP_REOVD]] RNA-directed RNA polymerase that is involved in transcription and genome replication. Following infection, it catalyzes the synthesis of fully conservative plus strands. After core assembly, which consists in recruitment of one capped plus-strand for each genomic segments and polymerase complexes, the polymerase switches mode and catalyzes the synthesis of complementary minus-strands.
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The reovirus polymerase and those of other dsRNA viruses function within the confines of a protein capsid to transcribe the tightly packed dsRNA genome segments. The crystal structure of the reovirus polymerase, lambda3, determined at 2.5 A resolution, shows a fingers-palm-thumb core, similar to those of other viral polymerases, surrounded by major N- and C-terminal elaborations, which create a cage-like structure, with four channels leading to the catalytic site. This "caged" polymerase has allowed us to visualize the results of several rounds of RNA polymerization directly in the crystals. A 5' cap binding site on the surface of lambda3 suggests a template retention mechanism by which attachment of the 5' end of the plus-sense strand facilitates insertion of the 3' end of the minus-sense strand into the template channel.
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RNA synthesis in a cage--structural studies of reovirus polymerase lambda3.,Tao Y, Farsetta DL, Nibert ML, Harrison SC Cell. 2002 Nov 27;111(5):733-45. PMID:12464184<ref>PMID:12464184</ref>
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==See Also==
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*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1n38" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Mammalian orthoreovirus 3 strain dearing]]
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[[Category: Mammalian orthoreovirus 3 Dearing]]
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[[Category: Farsetta, D L]]
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[[Category: Farsetta DL]]
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[[Category: Harrison, S C]]
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[[Category: Harrison SC]]
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[[Category: Nibert, M L]]
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[[Category: Nibert ML]]
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[[Category: Tao, Y]]
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[[Category: Tao Y]]
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[[Category: Bracelet]]
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[[Category: Right hand configuration]]
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[[Category: Rna polymerase]]
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[[Category: Transferase-rna complex]]
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Revision as of 17:00, 7 September 2022

reovirus polymerase lambda3 elongation complex with one phosphodiester bond formed

PDB ID 1n38

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