4wsa: Difference between revisions
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==Crystal structure of Influenza B polymerase bound to the vRNA promoter (FluB1 form)== | ==Crystal structure of Influenza B polymerase bound to the vRNA promoter (FluB1 form)== | ||
<StructureSection load='4wsa' size='340' side='right' caption='[[4wsa]], [[Resolution|resolution]] 3.40Å' scene=''> | <StructureSection load='4wsa' size='340' side='right'caption='[[4wsa]], [[Resolution|resolution]] 3.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4wsa]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WSA OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4wsa]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_B_virus Influenza B virus] and [https://en.wikipedia.org/wiki/Influenza_B_virus_(B/Memphis/13/2003) Influenza B virus (B/Memphis/13/2003)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WSA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WSA FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.4Å</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=4wsa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wsa OCA], [https://pdbe.org/4wsa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wsa RCSB], [https://www.ebi.ac.uk/pdbsum/4wsa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wsa ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5V8Z9_9INFB Q5V8Z9_9INFB] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4wsa" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[RNA polymerase 3D structures|RNA polymerase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Influenza B virus]] | ||
[[Category: Cusack | [[Category: Large Structures]] | ||
[[Category: Guilligay | [[Category: Cusack S]] | ||
[[Category: Pflug | [[Category: Guilligay D]] | ||
[[Category: Reich | [[Category: Pflug A]] | ||
[[Category: Reich S]] | |||
Latest revision as of 14:28, 9 May 2024
Crystal structure of Influenza B polymerase bound to the vRNA promoter (FluB1 form)Crystal structure of Influenza B polymerase bound to the vRNA promoter (FluB1 form)
Structural highlights
FunctionPublication Abstract from PubMedInfluenza virus polymerase uses a capped primer, derived by 'cap-snatching' from host pre-messenger RNA, to transcribe its RNA genome into mRNA and a stuttering mechanism to generate the poly(A) tail. By contrast, genome replication is unprimed and generates exact full-length copies of the template. Here we use crystal structures of bat influenza A and human influenza B polymerases (FluA and FluB), bound to the viral RNA promoter, to give mechanistic insight into these distinct processes. In the FluA structure, a loop analogous to the priming loop of flavivirus polymerases suggests that influenza could initiate unprimed template replication by a similar mechanism. Comparing the FluA and FluB structures suggests that cap-snatching involves in situ rotation of the PB2 cap-binding domain to direct the capped primer first towards the endonuclease and then into the polymerase active site. The polymerase probably undergoes considerable conformational changes to convert the observed pre-initiation state into the active initiation and elongation states. Structural insight into cap-snatching and RNA synthesis by influenza polymerase.,Reich S, Guilligay D, Pflug A, Malet H, Berger I, Crepin T, Hart D, Lunardi T, Nanao M, Ruigrok RW, Cusack S Nature. 2014 Nov 19. doi: 10.1038/nature14009. PMID:25409151[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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