3IG9

Small outer capsid protein (SOC) of bacteriophage RB69

Summary for 3IG9

• Entry DOI: 10.2210/pdb3ig9/pdb
• Related: 3IGE
• Descriptor: Soc small outer capsid protein, IMIDAZOLE (3 entities in total)
• Functional Keywords: alpha/beta structure, viral protein
• Biological source: Enterobacteria phage RB69 (Bacteriophage RB69)
• Total number of polymer chains: 4
• Total formula weight: 34530.47

Authors

Li, Q.,Fokine, A.,O'Donnell, E.,Rao, V.B.,Rossmann, M.G. (deposition date: 2009-07-27, release date: 2009-12-08, Last modification date: 2024-02-21)

Primary citation

Qin, L.,Fokine, A.,O'Donnell, E.,Rao, V.B.,Rossmann, M.G.
Structure of the Small Outer Capsid Protein, Soc: A Clamp for Stabilizing Capsids of T4-like Phages
J.Mol.Biol., 395:728-741, 2010

PubMed Abstract: Many viruses need to stabilize their capsid structure against DNA pressure and for survival in hostile environments. The 9-kDa outer capsid protein (Soc) of bacteriophage T4, which stabilizes the virus, attaches to the capsid during the final stage of maturation. There are 870 Soc molecules that act as a "glue" between neighboring hexameric capsomers, forming a "cage" that stabilizes the T4 capsid against extremes of pH and temperature. Here we report a 1.9 A resolution crystal structure of Soc from the bacteriophage RB69, a close relative of T4. The RB69 crystal structure and a homology model of T4 Soc were fitted into the cryoelectron microscopy reconstruction of the T4 capsid. This established the region of Soc that interacts with the major capsid protein and suggested a mechanism, verified by extensive mutational and biochemical studies, for stabilization of the capsid in which the Soc trimers act as clamps between neighboring capsomers. The results demonstrate the factors involved in stabilizing not only the capsids of T4-like bacteriophages but also many other virus capsids.

PubMed: 19835886
DOI: 10.1016/j.jmb.2009.10.007

Experimental method

X-RAY DIFFRACTION (1.9 Å)