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5FJ7

Structure of the P2 polymerase inside in vitro assembled bacteriophage phi6 polymerase complex, with P1 included

Summary for 5FJ7
Entry DOI10.2210/pdb5fj7/pdb
Related5FJ5 5FJ6
EMDB information3187
DescriptorMAJOR INNER PROTEIN P1, RNA-DIRECTED RNA POLYMERASE, MANGANESE (II) ION (3 entities in total)
Functional Keywordsviral protein, bacteriophage phi6, polymerase complex, p2, polymerase, p1
Biological sourcePSEUDOMONAS PHAGE PHI6
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Total number of polymer chains3
Total formula weight243285.49
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 citationIlca, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (7.9 Å)
Structure validation

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