3IZG
Bacteriophage T7 prohead shell EM-derived atomic model
Summary for 3IZG
Entry DOI | 10.2210/pdb3izg/pdb |
EMDB information | 1321 |
Descriptor | Major capsid protein 10A (1 entity in total) |
Functional Keywords | bacteriophage, virus, capsid maturation, cryoelectron microscopy, morphogenetic intermediate, icosahedral |
Biological source | Enterobacteria phage T7 (Bacteriophage T7) |
Total number of polymer chains | 7 |
Total formula weight | 256127.38 |
Authors | Ionel, A.,Velazquez-Muriel, J.A.,Agirrezabala, X.,Luque, D.,Cuervo, A.,Caston, J.R.,Valpuesta, J.M.,Martin-Benito, J.,Carrascosa, J.L. (deposition date: 2010-10-27, release date: 2010-11-17, Last modification date: 2024-02-21) |
Primary citation | Ionel, A.,Velazquez-Muriel, J.A.,Luque, D.,Cuervo, A.,Caston, J.R.,Valpuesta, J.M.,Martin-Benito, J.,Carrascosa, J.L. Molecular rearrangements involved in the capsid shell maturation of bacteriophage T7. J.Biol.Chem., 286:234-242, 2011 Cited by PubMed Abstract: Maturation of dsDNA bacteriophages involves assembling the virus prohead from a limited set of structural components followed by rearrangements required for the stability that is necessary for infecting a host under challenging environmental conditions. Here, we determine the mature capsid structure of T7 at 1 nm resolution by cryo-electron microscopy and compare it with the prohead to reveal the molecular basis of T7 shell maturation. The mature capsid presents an expanded and thinner shell, with a drastic rearrangement of the major protein monomers that increases in their interacting surfaces, in turn resulting in a new bonding lattice. The rearrangements include tilting, in-plane rotation, and radial expansion of the subunits, as well as a relative bending of the A- and P-domains of each subunit. The unique features of this shell transformation, which does not employ the accessory proteins, inserted domains, or molecular interactions observed in other phages, suggest a simple capsid assembling strategy that may have appeared early in the evolution of these viruses. PubMed: 20962334DOI: 10.1074/jbc.M110.187211 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (10.9 Å) |
Structure validation
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