2YMN

Organization of the Influenza Virus Replication Machinery

Summary for 2YMN

• Entry DOI: 10.2210/pdb2ymn/pdb
• EMDB information: 2209
• Descriptor: NUCLEOPROTEIN (1 entity in total)
• Functional Keywords: viral protein, rnp, polymerase
• Biological source: INFLUENZA A VIRUS (A/PUERTO RICO/8/1934(H1N1))
• Total number of polymer chains: 6
• Total formula weight: 338728.76

Authors

Moeller, A.,Kirchdoerfer, R.N.,Potter, C.S.,Carragher, B.,Wilson, I.A. (deposition date: 2012-10-09, release date: 2012-12-05, Last modification date: 2024-05-08)

Primary citation

Moeller, A.,Kirchdoerfer, R.N.,Potter, C.S.,Carragher, B.,Wilson, I.A.
Organization of the Influenza Virus Replication Machinery.
Science, 338:1631-, 2012

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.

PubMed: 23180774
DOI: 10.1126/SCIENCE.1227270

Experimental method

ELECTRON MICROSCOPY (20 Å)