2YMN

Organization of the Influenza Virus Replication Machinery


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 20.0 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: HELICAL 

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This is version 1.2 of the entry. See complete history


Literature

Organization of the Influenza Virus Replication Machinery.

Moeller, A.Kirchdoerfer, R.N.Potter, C.S.Carragher, B.Wilson, I.A.

(2012) Science 338: 1631

  • DOI: https://doi.org/10.1126/science.1227270
  • Primary Citation of Related Structures:  
    2YMN

  • PubMed Abstract: 

    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.


  • Organizational Affiliation

    National Resource for Automated Molecular Microscopy, Department of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
NUCLEOPROTEIN
A, B, C, D, E
A, B, C, D, E, F
498Influenza A virus (A/Puerto Rico/8/1934(H1N1))Mutation(s): 0 
UniProt
Find proteins for Q1K9H2 (Influenza A virus (strain A/Wilson-Smith/1933 H1N1))
Explore Q1K9H2 
Go to UniProtKB:  Q1K9H2
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ1K9H2
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 20.0 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: HELICAL 
EM Software:
TaskSoftware PackageVersion
RECONSTRUCTIONAppion
RECONSTRUCTIONIHRSR
RECONSTRUCTIONIMAGIC
RECONSTRUCTIONSPIDER
RECONSTRUCTIONXmipp

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2012-12-05
    Type: Initial release
  • Version 1.1: 2013-01-16
    Changes: Database references
  • Version 1.2: 2017-08-23
    Changes: Data collection