skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Structure of the Small Outer Capsid Protein, Soc: A Clamp for Stabilizing Capsids of T4-like Phages

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 {angstrom} 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.

Authors:
; ; ; ;  [1];  [2]
  1. (CUA)
  2. (
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
USDOE
OSTI Identifier:
1002259
Resource Type:
Journal Article
Resource Relation:
Journal Name: J. Mol. Biol.; Journal Volume: 395; Journal Issue: (4) ; 01, 2010
Country of Publication:
United States
Language:
ENGLISH
Subject:
36 MATERIALS SCIENCE; BACTERIOPHAGES; CRYSTAL STRUCTURE; DNA; MICROSCOPY; PROTEINS; RESOLUTION; STABILIZATION; VIRUSES

Citation Formats

Qin, Li, Fokine, Andrei, O'Donnell, Erin, Rao, Venigalla B., Rossmann, Michael G., and Purdue). Structure of the Small Outer Capsid Protein, Soc: A Clamp for Stabilizing Capsids of T4-like Phages. United States: N. p., 2010. Web. doi:10.1016/j.jmb.2009.10.007.
Qin, Li, Fokine, Andrei, O'Donnell, Erin, Rao, Venigalla B., Rossmann, Michael G., & Purdue). Structure of the Small Outer Capsid Protein, Soc: A Clamp for Stabilizing Capsids of T4-like Phages. United States. doi:10.1016/j.jmb.2009.10.007.
Qin, Li, Fokine, Andrei, O'Donnell, Erin, Rao, Venigalla B., Rossmann, Michael G., and Purdue). Thu . "Structure of the Small Outer Capsid Protein, Soc: A Clamp for Stabilizing Capsids of T4-like Phages". United States. doi:10.1016/j.jmb.2009.10.007.
@article{osti_1002259,
title = {Structure of the Small Outer Capsid Protein, Soc: A Clamp for Stabilizing Capsids of T4-like Phages},
author = {Qin, Li and Fokine, Andrei and O'Donnell, Erin and Rao, Venigalla B. and Rossmann, Michael G. and Purdue)},
abstractNote = {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 {angstrom} 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.},
doi = {10.1016/j.jmb.2009.10.007},
journal = {J. Mol. Biol.},
number = (4) ; 01, 2010,
volume = 395,
place = {United States},
year = {Thu Jul 22 00:00:00 EDT 2010},
month = {Thu Jul 22 00:00:00 EDT 2010}
}