6z5l

From Proteopedia

(Difference between revisions)

Current revision

Helical reconstruction of influenza A virus M1 in complex with nucleic acid.

Structural highlights

6z5l is a 1 chain structure with sequence from Influenza A virus (A/Puerto Rico/8/1934(H1N1)). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.8Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

M1_I34A1 Plays critical roles in virus replication, from virus entry and uncoating to assembly and budding of the virus particle. M1 binding to ribonucleocapsids (RNPs) in nucleus seems to inhibit viral transcription. Interaction of viral NEP with M1-RNP is thought to promote nuclear export of the complex, which is targeted to the virion assembly site at the apical plasma membrane in polarized epithelial cells. Interactions with NA and HA may bring M1, a non-raft-associated protein, into lipid rafts. Forms a continuous shell on the inner side of the lipid bilayer in virion, where it binds the RNP. During virus entry into cell, the M2 ion channel acidifies the internal virion core, inducing M1 dissociation from the RNP. M1-free RNPs are transported to the nucleus, where viral transcription and replication can take place.^[1] Determines the virion's shape: spherical or filamentous. Clinical isolates of influenza are characterized by the presence of significant proportion of filamentous virions, whereas after multiple passage on eggs or cell culture, virions have only spherical morphology. Filamentous virions are thought to be important to infect neighboring cells, and spherical virions more suited to spread through aerosol between hosts organisms.^[2]

Publication Abstract from PubMed

Influenza A virus causes millions of severe cases of disease during annual epidemics. The most abundant protein in influenza virions is matrix protein 1 (M1), which mediates virus assembly by forming an endoskeleton beneath the virus membrane(1). The structure of full-length M1, and how it oligomerizes to mediate the assembly of virions, is unknown. Here we determine the complete structure of assembled M1 within intact virus particles, as well as the structure of M1 oligomers reconstituted in vitro. We find that the C-terminal domain of M1 is disordered in solution but can fold and bind in trans to the N-terminal domain of another M1 monomer, thus polymerizing M1 into linear strands that coat the interior surface of the membrane of the assembling virion. In the M1 polymer, five histidine residues-contributed by three different monomers of M1-form a cluster that can serve as the pH-sensitive disassembly switch after entry into a target cell. These structures therefore reveal mechanisms of influenza virus assembly and disassembly.

The native structure of the assembled matrix protein 1 of influenza A virus.,Peukes J, Xiong X, Erlendsson S, Qu K, Wan W, Calder LJ, Schraidt O, Kummer S, Freund SMV, Krausslich HG, Briggs JAG Nature. 2020 Sep 9. pii: 10.1038/s41586-020-2696-8. doi:, 10.1038/s41586-020-2696-8. PMID:32908308^[3]

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

References

↑ Huang X, Liu T, Muller J, Levandowski RA, Ye Z. Effect of influenza virus matrix protein and viral RNA on ribonucleoprotein formation and nuclear export. Virology. 2001 Sep 1;287(2):405-16. PMID:11531417 doi:10.1006/viro.2001.1067
↑ Huang X, Liu T, Muller J, Levandowski RA, Ye Z. Effect of influenza virus matrix protein and viral RNA on ribonucleoprotein formation and nuclear export. Virology. 2001 Sep 1;287(2):405-16. PMID:11531417 doi:10.1006/viro.2001.1067
↑ Peukes J, Xiong X, Erlendsson S, Qu K, Wan W, Calder LJ, Schraidt O, Kummer S, Freund SMV, Krausslich HG, Briggs JAG. The native structure of the assembled matrix protein 1 of influenza A virus. Nature. 2020 Sep 9. pii: 10.1038/s41586-020-2696-8. doi:, 10.1038/s41586-020-2696-8. PMID:32908308 doi:http://dx.doi.org/10.1038/s41586-020-2696-8

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6z5l"

Categories: Large Structures | Briggs JAG | Qu K | Xiong X

@@ Line 3: / Line 3: @@
 <StructureSection load='6z5l' size='340' side='right'caption='[[6z5l]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6z5l]] is a 1 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=6Z5L OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6Z5L FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6z5l]] is a 1 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=6Z5L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Z5L 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=6z5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6z5l OCA], [http://pdbe.org/6z5l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6z5l RCSB], [http://www.ebi.ac.uk/pdbsum/6z5l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6z5l ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.8&#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=6z5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6z5l OCA], [https://pdbe.org/6z5l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6z5l RCSB], [https://www.ebi.ac.uk/pdbsum/6z5l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6z5l ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/M1_I34A1 M1_I34A1]] Plays critical roles in virus replication, from virus entry and uncoating to assembly and budding of the virus particle. M1 binding to ribonucleocapsids (RNPs) in nucleus seems to inhibit viral transcription. Interaction of viral NEP with M1-RNP is thought to promote nuclear export of the complex, which is targeted to the virion assembly site at the apical plasma membrane in polarized epithelial cells. Interactions with NA and HA may bring M1, a non-raft-associated protein, into lipid rafts. Forms a continuous shell on the inner side of the lipid bilayer in virion, where it binds the RNP. During virus entry into cell, the M2 ion channel acidifies the internal virion core, inducing M1 dissociation from the RNP. M1-free RNPs are transported to the nucleus, where viral transcription and replication can take place.<ref>PMID:11531417</ref>   Determines the virion's shape: spherical or filamentous. Clinical isolates of influenza are characterized by the presence of significant proportion of filamentous virions, whereas after multiple passage on eggs or cell culture, virions have only spherical morphology. Filamentous virions are thought to be important to infect neighboring cells, and spherical virions more suited to spread through aerosol between hosts organisms.<ref>PMID:11531417</ref>
+[https://www.uniprot.org/uniprot/M1_I34A1 M1_I34A1] Plays critical roles in virus replication, from virus entry and uncoating to assembly and budding of the virus particle. M1 binding to ribonucleocapsids (RNPs) in nucleus seems to inhibit viral transcription. Interaction of viral NEP with M1-RNP is thought to promote nuclear export of the complex, which is targeted to the virion assembly site at the apical plasma membrane in polarized epithelial cells. Interactions with NA and HA may bring M1, a non-raft-associated protein, into lipid rafts. Forms a continuous shell on the inner side of the lipid bilayer in virion, where it binds the RNP. During virus entry into cell, the M2 ion channel acidifies the internal virion core, inducing M1 dissociation from the RNP. M1-free RNPs are transported to the nucleus, where viral transcription and replication can take place.<ref>PMID:11531417</ref>   Determines the virion's shape: spherical or filamentous. Clinical isolates of influenza are characterized by the presence of significant proportion of filamentous virions, whereas after multiple passage on eggs or cell culture, virions have only spherical morphology. Filamentous virions are thought to be important to infect neighboring cells, and spherical virions more suited to spread through aerosol between hosts organisms.<ref>PMID:11531417</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: I34a1]]
 [[Category: Large Structures]]
-[[Category: Briggs, J A.G]]
+[[Category: Briggs JAG]]
-[[Category: Qu, K]]
+[[Category: Qu K]]
-[[Category: Xiong, X]]
+[[Category: Xiong X]]
-[[Category: Assembly]]
-[[Category: Influenza virus]]
-[[Category: M1]]
-[[Category: Matrix protein]]
-[[Category: Ribonucleoprotein complex]]
-[[Category: Viral protein]]

6z5l

From Proteopedia

Current revision

Helical reconstruction of influenza A virus M1 in complex with nucleic acid.

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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