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3IZG

Bacteriophage T7 prohead shell EM-derived atomic model

Summary for 3IZG
Entry DOI10.2210/pdb3izg/pdb
EMDB information1321
DescriptorMajor capsid protein 10A (1 entity in total)
Functional Keywordsbacteriophage, virus, capsid maturation, cryoelectron microscopy, morphogenetic intermediate, icosahedral
Biological sourceEnterobacteria phage T7 (Bacteriophage T7)
Total number of polymer chains7
Total formula weight256127.38
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 citationIonel, 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: 20962334
DOI: 10.1074/jbc.M110.187211
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (10.9 Å)
Structure validation

235183

数据于2025-04-23公开中

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