2ztt: Difference between revisions
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==Crystal Structure of RNA polymerase PB1-PB2 subunits from Influenza A Virus== | ==Crystal Structure of RNA polymerase PB1-PB2 subunits from Influenza A Virus== | ||
<StructureSection load='2ztt' size='340' side='right' caption='[[2ztt]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='2ztt' size='340' side='right'caption='[[2ztt]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2ztt]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2ztt]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/I34a1 I34a1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZTT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZTT FirstGlance]. <br> | ||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PB1 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PB1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=211044 I34A1]), PB2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=211044 I34A1])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/RNA-directed_RNA_polymerase RNA-directed RNA polymerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.48 2.7.7.48] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ztt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ztt OCA], [https://pdbe.org/2ztt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ztt RCSB], [https://www.ebi.ac.uk/pdbsum/2ztt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ztt ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/RDRP_I34A1 RDRP_I34A1]] RNA-dependent RNA polymerase which is responsible for replication and transcription of virus segments. Binds the promoter sequence of the encapsidated viral RNA. Displays an endonuclease activity involved in cap-stealing. Cleaves cellular pre-mRNA to generate primers for viral transcription. [[https://www.uniprot.org/uniprot/PB2_I34A1 PB2_I34A1]] Involved in transcription initiation and cap-stealing mechanism, in which cellular capped pre-mRNA are used to generate primers for viral transcription. Binds the cap of the target pre-RNA which is subsequently cleaved by PB1. May play a role in genome replication (By similarity). | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[RNA polymerase|RNA polymerase]] | *[[RNA polymerase 3D structures|RNA polymerase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: I34a1]] | [[Category: I34a1]] | ||
[[Category: Large Structures]] | |||
[[Category: RNA-directed RNA polymerase]] | [[Category: RNA-directed RNA polymerase]] | ||
[[Category: Obayashi, E]] | [[Category: Obayashi, E]] | ||
Revision as of 20:37, 15 December 2021
Crystal Structure of RNA polymerase PB1-PB2 subunits from Influenza A VirusCrystal Structure of RNA polymerase PB1-PB2 subunits from Influenza A Virus
Structural highlights
Function[RDRP_I34A1] RNA-dependent RNA polymerase which is responsible for replication and transcription of virus segments. Binds the promoter sequence of the encapsidated viral RNA. Displays an endonuclease activity involved in cap-stealing. Cleaves cellular pre-mRNA to generate primers for viral transcription. [PB2_I34A1] Involved in transcription initiation and cap-stealing mechanism, in which cellular capped pre-mRNA are used to generate primers for viral transcription. Binds the cap of the target pre-RNA which is subsequently cleaved by PB1. May play a role in genome replication (By similarity). Publication Abstract from PubMedInfluenza virus RNA-dependent RNA polymerase is a multi-functional heterotrimer, which uses a 'cap-snatching' mechanism to produce viral mRNA. Host cell mRNA is cleaved to yield a cap-bearing oligonucleotide, which can be extended using viral genomic RNA as a template. The cap-binding and endonuclease activities are only activated once viral genomic RNA is bound. This requires signalling from the RNA-binding PB1 subunit to the cap-binding PB2 subunit, and the interface between these two subunits is essential for the polymerase activity. We have defined this interaction surface by protein crystallography and tested the effects of mutating contact residues on the function of the holo-enzyme. This novel interface is surprisingly small, yet, it has a crucial function in regulating the 250 kDa polymerase complex and is completely conserved among avian and human influenza viruses. Structural insight into the essential PB1-PB2 subunit contact of the influenza virus RNA polymerase.,Sugiyama K, Obayashi E, Kawaguchi A, Suzuki Y, Tame JR, Nagata K, Park SY EMBO J. 2009 Jun 17;28(12):1803-11. Epub 2009 May 21. PMID:19461581[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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