Display Settings:

Format

Send to:

Choose Destination
See comment in PubMed Commons below
Virology. 2010 Jun 5;401(2):119-30. doi: 10.1016/j.virol.2010.02.017. Epub 2010 Mar 16.

'Let the phage do the work': using the phage P22 coat protein structures as a framework to understand its folding and assembly mutants.

Author information

  • 1Department of Molecular and Cell Biology, 91 N. Eagleville Rd., U-3125, University of Connecticut, Storrs, CT 06269-3125, USA. Teschke@uconn.edu

Abstract

The amino acid sequence of viral capsid proteins contains information about their folding, structure and self-assembly processes. While some viruses assemble from small preformed oligomers of coat proteins, other viruses such as phage P22 and herpesvirus assemble from monomeric proteins (Fuller and King, 1980; Newcomb et al., 1999). The subunit assembly process is strictly controlled through protein:protein interactions such that icosahedral structures are formed with specific symmetries, rather than aberrant structures. dsDNA viruses commonly assemble by first forming a precursor capsid that serves as a DNA packaging machine (Earnshaw, Hendrix, and King, 1980; Heymann et al., 2003). DNA packaging is accompanied by a conformational transition of the small precursor procapsid into a larger capsid for isometric viruses. Here we highlight the pseudo-atomic structures of phage P22 coat protein and rationalize several decades of data about P22 coat protein folding, assembly and maturation generated from a combination of genetics and biochemistry.

2010 Elsevier Inc. All rights reserved.

PMID:
20236676
[PubMed - indexed for MEDLINE]
PMCID:
PMC2862144
Free PMC Article

Images from this publication.See all images (6)Free text

Figure 1
Figure 2
Figure 3
Figure 4
Figure 5
Figure 6
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science Icon for PubMed Central
    Loading ...
    Write to the Help Desk