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| | <StructureSection load='2znl' size='340' side='right'caption='[[2znl]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='2znl' size='340' side='right'caption='[[2znl]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2znl]] is a 2 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=2ZNL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZNL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2znl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/Puerto_Rico/8/1934(H1N1)) Influenza A virus (A/Puerto Rico/8/1934(H1N1))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZNL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZNL FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=211044 I34A1]), PB1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=211044 I34A1])</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]] 2.3Å</td></tr> |
| - | <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'>[https://proteopedia.org/fgij/fg.htm?mol=2znl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2znl OCA], [https://pdbe.org/2znl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2znl RCSB], [https://www.ebi.ac.uk/pdbsum/2znl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2znl 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=2znl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2znl OCA], [https://pdbe.org/2znl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2znl RCSB], [https://www.ebi.ac.uk/pdbsum/2znl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2znl ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/PA_I34A1 PA_I34A1]] Implicated in endonuclease cleavage of capped RNA primers. Displays an elongation factor activity in viral RNA synthesis. Dispensable for viral transcription, but not replication. [[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/PA_I34A1 PA_I34A1] Implicated in endonuclease cleavage of capped RNA primers. Displays an elongation factor activity in viral RNA synthesis. Dispensable for viral transcription, but not replication. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: I34a1]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: RNA-directed RNA polymerase]]
| + | [[Category: Kawaguchi A]] |
| - | [[Category: Kawaguchi, A]] | + | [[Category: Kawai F]] |
| - | [[Category: Kawai, F]] | + | [[Category: Nagata K]] |
| - | [[Category: Nagata, K]] | + | [[Category: Obayashi E]] |
| - | [[Category: Obayashi, E]] | + | [[Category: Park S-Y]] |
| - | [[Category: Park, S Y]] | + | [[Category: Shibayama N]] |
| - | [[Category: Shibayama, N]] | + | [[Category: Tame JRH]] |
| - | [[Category: Tame, J R.H]] | + | [[Category: Yoshida H]] |
| - | [[Category: Yoshida, H]] | + | |
| - | [[Category: Influenza a virus]]
| + | |
| - | [[Category: Nucleotide-binding]]
| + | |
| - | [[Category: Nucleotidyltransferase]]
| + | |
| - | [[Category: Pa]]
| + | |
| - | [[Category: Pb1]]
| + | |
| - | [[Category: Phosphoprotein]]
| + | |
| - | [[Category: Rna polymerase]]
| + | |
| - | [[Category: Rna replication]]
| + | |
| - | [[Category: Rna-directed rna polymerase]]
| + | |
| - | [[Category: Subunit interaction]]
| + | |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
PA_I34A1 Implicated in endonuclease cleavage of capped RNA primers. Displays an elongation factor activity in viral RNA synthesis. Dispensable for viral transcription, but not replication.
Publication Abstract from PubMed
Influenza A virus is a major human and animal pathogen with the potential to cause catastrophic loss of life. The virus reproduces rapidly, mutates frequently and occasionally crosses species barriers. The recent emergence in Asia of avian influenza related to highly pathogenic forms of the human virus has highlighted the urgent need for new effective treatments. Here we demonstrate the importance to viral replication of a subunit interface in the viral RNA polymerase, thereby providing a new set of potential drug binding sites entirely independent of surface antigen type. No current medication targets this heterotrimeric polymerase complex. All three subunits, PB1, PB2 and PA, are required for both transcription and replication. PB1 carries the polymerase active site, PB2 includes the capped-RNA recognition domain, and PA is involved in assembly of the functional complex, but so far very little structural information has been reported for any of them. We describe the crystal structure of a large fragment of one subunit (PA) of influenza A RNA polymerase bound to a fragment of another subunit (PB1). The carboxy-terminal domain of PA forms a novel fold, and forms a deep, highly hydrophobic groove into which the amino-terminal residues of PB1 can fit by forming a 3(10) helix.
The structural basis for an essential subunit interaction in influenza virus RNA polymerase.,Obayashi E, Yoshida H, Kawai F, Shibayama N, Kawaguchi A, Nagata K, Tame JR, Park SY Nature. 2008 Aug 28;454(7208):1127-31. Epub 2008 Jul 27. PMID:18660801[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Obayashi E, Yoshida H, Kawai F, Shibayama N, Kawaguchi A, Nagata K, Tame JR, Park SY. The structural basis for an essential subunit interaction in influenza virus RNA polymerase. Nature. 2008 Aug 28;454(7208):1127-31. Epub 2008 Jul 27. PMID:18660801 doi:nature07225
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