2XVR

Phage T7 empty mature head shell

Summary for 2XVR

• Entry DOI: 10.2210/pdb2xvr/pdb
• EMDB information: 1810
• Descriptor: MAJOR CAPSID PROTEIN 10A (1 entity in total)
• Functional Keywords: virus, capsid maturation, morphogenetic intermediate
• Biological source: ENTEROBACTERIA PHAGE T7
• Total number of polymer chains: 7
• Total formula weight: 256127.38

Authors

Ionel, A.,Velazquez-Muriel, J.A.,Luque, D.,Cuervo, A.,Caston, J.R.,Valpuesta, J.M.,Martin-Benito, J.,Carrascosa, J.L. (deposition date: 2010-10-28, release date: 2010-12-01, Last modification date: 2024-05-08)

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-, 2011

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

Experimental method

ELECTRON MICROSCOPY (10.8 Å)