2ymn

From Proteopedia

(Difference between revisions)

Revision as of 10:39, 12 January 2022

Organization of the Influenza Virus Replication Machinery

2ymn, resolution 20.00Å

Structural highlights

2ymn is a 6 chain structure with sequence from I34a1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[Q1I2B5_9INFA] Encapsidates the negative strand viral RNA, protecting it from nucleases. The encapsidated genomic RNA is termed the ribonucleoprotein (RNP) and serves as template for transcription and replication. The RNP needs to be localized in the nucleus to start an infectious cycle, but is too large to diffuse through the nuclear pore complex. NP comprises at least 2 nuclear localization signals and is responsible of the active RNP import into the nucleus through the cellular importin alpha/beta pathway. Later in the infection, nucleus export of RNP are mediated through viral proteins NEP interacting with M1 which binds nucleoproteins. It is possible that the nucleoprotein binds directly exportin-1 (XPO1) and plays an active role in RNP nuclear export. M1 interaction with RNP seems to hide nucleoprotein's nuclear localization signals. Soon after a virion infects a new cell, M1 dissociates from the RNP under acidification of the virion driven by M2 protein. Dissociation of M1 from RNP unmask nucleoprotein's nuclear localization signals, targeting the RNP to the nucleus (By similarity).[SAAS:SAAS00208116]

Publication Abstract from PubMed

Influenza virus ribonucleoprotein complexes (RNPs) are central to the viral life cycle and in adaptation to new host species. RNPs are composed of the viral genome, viral polymerase, and many copies of the viral nucleoprotein. In vitro cell expression of all RNP protein components with four of the eight influenza virus gene segments enabled structural determination of native influenza virus RNPs by means of cryogenic electron microscopy (cryo-EM). The cryo-EM structure reveals the architecture and organization of the native RNP, defining the attributes of its largely helical structure and how polymerase interacts with nucleoprotein and the viral genome. Observations of branched-RNP structures in negative-stain electron microscopy and their putative identification as replication intermediates suggest a mechanism for viral replication by a second polymerase on the RNP template.

Organization of the influenza virus replication machinery.,Moeller A, Kirchdoerfer RN, Potter CS, Carragher B, Wilson IA Science. 2012 Dec 21;338(6114):1631-4. doi: 10.1126/science.1227270. Epub 2012, Nov 22. PMID:23180774^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Moeller A, Kirchdoerfer RN, Potter CS, Carragher B, Wilson IA. Organization of the influenza virus replication machinery. Science. 2012 Dec 21;338(6114):1631-4. doi: 10.1126/science.1227270. Epub 2012, Nov 22. PMID:23180774 doi:http://dx.doi.org/10.1126/science.1227270

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ymn"

@@ Line 3: / Line 3: @@
 <SX load='2ymn' size='340' side='right' viewer='molstar' caption='[[2ymn]], [[Resolution|resolution]] 20.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2ymn]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/I34a1 I34a1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YMN OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2YMN FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2ymn]] is a 6 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=2YMN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YMN FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2ymn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ymn OCA], [http://pdbe.org/2ymn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ymn RCSB], [http://www.ebi.ac.uk/pdbsum/2ymn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ymn ProSAT]</span></td></tr>
+</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=2ymn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ymn OCA], [https://pdbe.org/2ymn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ymn RCSB], [https://www.ebi.ac.uk/pdbsum/2ymn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ymn ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/Q1I2B5_9INFA Q1I2B5_9INFA]] Encapsidates the negative strand viral RNA, protecting it from nucleases. The encapsidated genomic RNA is termed the ribonucleoprotein (RNP) and serves as template for transcription and replication. The RNP needs to be localized in the nucleus to start an infectious cycle, but is too large to diffuse through the nuclear pore complex. NP comprises at least 2 nuclear localization signals and is responsible of the active RNP import into the nucleus through the cellular importin alpha/beta pathway. Later in the infection, nucleus export of RNP are mediated through viral proteins NEP interacting with M1 which binds nucleoproteins. It is possible that the nucleoprotein binds directly exportin-1 (XPO1) and plays an active role in RNP nuclear export. M1 interaction with RNP seems to hide nucleoprotein's nuclear localization signals. Soon after a virion infects a new cell, M1 dissociates from the RNP under acidification of the virion driven by M2 protein. Dissociation of M1 from RNP unmask nucleoprotein's nuclear localization signals, targeting the RNP to the nucleus (By similarity).[SAAS:SAAS00208116]
+[[https://www.uniprot.org/uniprot/Q1I2B5_9INFA Q1I2B5_9INFA]] Encapsidates the negative strand viral RNA, protecting it from nucleases. The encapsidated genomic RNA is termed the ribonucleoprotein (RNP) and serves as template for transcription and replication. The RNP needs to be localized in the nucleus to start an infectious cycle, but is too large to diffuse through the nuclear pore complex. NP comprises at least 2 nuclear localization signals and is responsible of the active RNP import into the nucleus through the cellular importin alpha/beta pathway. Later in the infection, nucleus export of RNP are mediated through viral proteins NEP interacting with M1 which binds nucleoproteins. It is possible that the nucleoprotein binds directly exportin-1 (XPO1) and plays an active role in RNP nuclear export. M1 interaction with RNP seems to hide nucleoprotein's nuclear localization signals. Soon after a virion infects a new cell, M1 dissociates from the RNP under acidification of the virion driven by M2 protein. Dissociation of M1 from RNP unmask nucleoprotein's nuclear localization signals, targeting the RNP to the nucleus (By similarity).[SAAS:SAAS00208116]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

2ymn

From Proteopedia

Revision as of 10:39, 12 January 2022

Organization of the Influenza Virus Replication Machinery

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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