3cw4: Difference between revisions

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 ==Large c-terminal domain of influenza a virus RNA-dependent polymerase PB2==
-<StructureSection load='3cw4' size='340' side='right' caption='[[3cw4]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
+<StructureSection load='3cw4' size='340' side='right'caption='[[3cw4]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3cw4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus Influenza a virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CW4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CW4 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3cw4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus Influenza A virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CW4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CW4 FirstGlance]. <br>
-</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=3cw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cw4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3cw4 RCSB], [http://www.ebi.ac.uk/pdbsum/3cw4 PDBsum]</span></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]] 2.7&#8491;</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=3cw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cw4 OCA], [https://pdbe.org/3cw4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cw4 RCSB], [https://www.ebi.ac.uk/pdbsum/3cw4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cw4 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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).
+[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;">
-== Publication Abstract from PubMed ==
-Because the influenza A virus has an RNA genome, its RNA-dependent RNA polymerase, comprising the PA, PB1, and PB2 subunits, is essential for viral transcription and replication. The binding of RNA primers/promoters to the polymerases is an initiation step in viral transcription. In our current study, we reveal the 2.7 A tertiary structure of the C-terminal RNA-binding domain of PB2 by x-ray crystallography. This domain incorporates lysine 627 of PB2, and this residue is associated with the high pathogenicity and host range restriction of influenza A virus. We found from our current analyses that this lysine is located in a unique "phi"-shaped structure consisting of a helix and an encircled loop within the PB2 domain. By electrostatic analysis, we identified a highly basic groove along with this phi loop and found that lysine 627 is located in the phi loop. A PB2 domain mutant in which glutamic acid is substituted at position 627 shows significantly lower RNA binding activity. This is the first report to show a relationship between RNA binding activity and the pathogenicity-determinant lysine 627. Using the Matras program for protein three-dimensional structural comparisons, we further found that the helix bundles in the PB2 domain are similar to that of activator 1, the 40-kDa subunit of DNA replication clamp loader (replication factor C), which is also an RNA-binding protein. This suggests a functional and structural relationship between the RNA-binding mechanisms underlying both influenza A viral transcription and cellular DNA replication. Our present results thus provide important new information for developing novel drugs that target the primer/promoter RNA binding of viral RNA polymerases.
-Structural basis of the influenza A virus RNA polymerase PB2 RNA-binding domain containing the pathogenicity-determinant lysine 627 residue.,Kuzuhara T, Kise D, Yoshida H, Horita T, Murazaki Y, Nishimura A, Echigo N, Utsunomiya H, Tsuge H J Biol Chem. 2009 Mar 13;284(11):6855-60. Epub 2009 Jan 14. PMID:19144639<ref>PMID:19144639</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
 ==See Also==
-*[[RNA polymerase|RNA polymerase]]
+*[[RNA polymerase 3D structures|RNA polymerase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Influenza a virus]]
+[[Category: Influenza A virus]]
-[[Category: Fujiki, H]]
+[[Category: Large Structures]]
-[[Category: Horita, T]]
+[[Category: Fujiki H]]
-[[Category: Kise, D]]
+[[Category: Horita T]]
-[[Category: Kuzuhara, T]]
+[[Category: Kise D]]
-[[Category: Murasaki, Y]]
+[[Category: Kuzuhara T]]
-[[Category: Tsuge, H]]
+[[Category: Murasaki Y]]
-[[Category: Utsunomiya, H]]
+[[Category: Tsuge H]]
-[[Category: Yoshida, H]]
+[[Category: Utsunomiya H]]
-[[Category: Mitochondrion]]
+[[Category: Yoshida H]]
-[[Category: Mrna capping]]
-[[Category: Mrna processing]]
-[[Category: Nucleus]]
-[[Category: Rna polymerase]]
-[[Category: Transferase]]
-[[Category: Virion]]