5FJ5

Structure of the in vitro assembled bacteriophage phi6 polymerase complex

Summary for 5FJ5

• Entry DOI: 10.2210/pdb5fj5/pdb
• Related: 5FJ6 5FJ7
• EMDB information: 3185
• Descriptor: MAJOR INNER PROTEIN P1 (1 entity in total)
• Functional Keywords: viral protein, polymerase complex
• Biological source: PSEUDOMONAS PHAGE PHI6
• Cellular location: Virion: P11126
• Total number of polymer chains: 2
• Total formula weight: 168327.34

Authors

Ilca, S.,Kotecha, A.,Sun, X.,Poranen, M.P.,Stuart, D.I.,Huiskonen, J.T. (deposition date: 2015-10-06, release date: 2015-11-04, Last modification date: 2024-05-08)

Primary citation

Ilca, S.L.,Kotecha, A.,Sun, X.,Poranen, M.M.,Stuart, D.I.,Huiskonen, J.T.
Localized Reconstruction of Subunits from Electron Cryomicroscopy Images of Macromolecular Complexes.
Nat.Commun., 6:8843-, 2015

PubMed Abstract: Electron cryomicroscopy can yield near-atomic resolution structures of highly ordered macromolecular complexes. Often however some subunits bind in a flexible manner, have different symmetry from the rest of the complex, or are present in sub-stoichiometric amounts, limiting the attainable resolution. Here we report a general method for the localized three-dimensional reconstruction of such subunits. After determining the particle orientations, local areas corresponding to the subunits can be extracted and treated as single particles. We demonstrate the method using three examples including a flexible assembly and complexes harbouring subunits with either partial occupancy or mismatched symmetry. Most notably, the method allows accurate fitting of the monomeric RNA-dependent RNA polymerase bound at the threefold axis of symmetry inside a viral capsid, revealing for the first time its exact orientation and interactions with the capsid proteins. Localized reconstruction is expected to provide novel biological insights in a range of challenging biological systems.

PubMed: 26534841
DOI: 10.1038/NCOMMS9843

Experimental method

ELECTRON MICROSCOPY (4.8 Å)