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Biomol NMR Assign. 2015 Oct;9(2):333-6. doi: 10.1007/s12104-015-9604-4. Epub 2015 Feb 19.

NMR assignments for the insertion domain of bacteriophage CUS-3 coat protein.

Author information

  • 1Department of Molecular & Cell Biology, and Chemistry, University of Connecticut, 91 N. Eagleville Road., Storrs, CT, 06269-3125, USA.
  • 2Department of Molecular, Microbial, and Structural Biology, University of Connecticut Health, 263 Farmington Ave., Farmington, CT, 06030-3305, USA.
  • 3Department of Molecular & Cell Biology, and Chemistry, University of Connecticut, 91 N. Eagleville Road., Storrs, CT, 06269-3125, USA. teschke@uconn.edu.
  • 4Department of Chemistry, University of Connecticut, 55 N. Eagleville Rd., Storrs, CT, 06269-3060, USA. teschke@uconn.edu.
  • 5Department of Molecular & Cell Biology, and Chemistry, University of Connecticut, 91 N. Eagleville Road., Storrs, CT, 06269-3125, USA. andrei@uconn.edu.

Abstract

CUS-3 is a P22-like tailed dsDNA bacteriophage that infects Escherichia coli serotype K1. The CUS-3 coat protein, which forms the icosahedral capsid, has a conserved HK97-fold but with a non-conserved accessory domain known as the insertion domain (I-domain). Sequence alignment of the coat proteins from CUS-3 and P22 shows higher sequence similarity for the I-domains (35 %) than for the HK97-cores, suggesting the I-domains play important functional roles. The I-domain of the P22 coat protein, which has an NMR structure comprised of a six-stranded β-barrel, has been shown to govern the assembly, stability and size of the resulting capsid particles. Here, we report the (1)H, (15)N, and (13)C assignments for the I-domain from the coat protein of bacteriophage CUS-3. The secondary structure and dynamics of the CUS-3 I-domain, predicted from the assigned NMR chemical shifts, agree with those of the P22 I-domain, suggesting the CUS-3 and P22 I-domains may have similar structures and functions in capsid assembly.

KEYWORDS:

Bacteriophage; CUS-3; I-domain; Procapsid; Viral assembly

PMID:
25694158
PMCID:
PMC4544682
DOI:
10.1007/s12104-015-9604-4
[PubMed - indexed for MEDLINE]
Free PMC Article
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