Advertisement

Biomolecular NMR Assignments

, Volume 9, Issue 2, pp 333–336 | Cite as

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

  • Therese N. Tripler
  • Mark W. Maciejewski
  • Carolyn M. TeschkeEmail author
  • Andrei T. AlexandrescuEmail author
Article

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 1H, 15N, and 13C 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 I-domain CUS-3 Viral assembly Procapsid 

Notes

Acknowledgments

We wish to thank Dr. K. Parent for supplying CUS-3 bacteriophage and Drs. A.D. Shuyker, M.R. Gryk, and J.C. Hoch for the use of the software platform NMRbox, http://nmrbox.org/, version 0.4a. This work was supported by NIH grant R01 GM076661 to C.M.T. and a supplement to C.M.T. and A.T.A.

Conflict of interest

The authors declare no conflict of interest.

Ethical standards

All experiments complied with all laws of the United States of America.

References

  1. Casjens SR, Thuman-Commike PA (2011) Evolution of mosaically related tailed bacteriophage genomes seen through the lens of phage P22 virion assembly. Virology 411:393–415. doi: 10.1016/j.virol.2010.12.046 CrossRefGoogle Scholar
  2. Cavanagh J, Fairbrother WJ, Palmer AG III, Rance M, Skelton NJ (2006) Protein NMR spectroscopy principles and practice. Protein NMR spectroscopy principles and practice, 2nd edn. Elsevier Inc., AmsterdamGoogle Scholar
  3. Cole C, Barber JD, Barton GJ (2008) The Jpred 3 secondary structure prediction server. Nucleic Acids Res 36:W197–W201CrossRefGoogle Scholar
  4. Parent KN, Gilcrease EB, Casjens SR, Baker TS (2012) Structural evolution of the P22-like phages: comparison of Sf6 and P22 procapsid and virion architectures. Virology 427:177–188. doi: 10.1016/j.virol.2012.01.040 CrossRefGoogle Scholar
  5. Parent KN et al (2014) Three-dimensional reconstructions of the bacteriophage CUS-3 virion reveal a conserved coat protein I-domain but a distinct tailspike receptor-binding domain. Virology 464–465:55–66. doi: 10.1016/j.virol.2014.06.017 CrossRefGoogle Scholar
  6. Rizzo AA et al (2014) Multiple functional roles of the accessory I-domain of bacteriophage P22 coat protein revealed by NMR structure and CryoEM modeling. Structure 22:830–841. doi: 10.1016/j.str.2014.04.003 CrossRefGoogle Scholar
  7. Shen Y, Delaglio F, Cornilescu G, Bax A (2009) TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J Biomol NMR 44:213–223. doi: 10.1007/s10858-009-9333-z CrossRefGoogle Scholar
  8. Suhanovsky MM, Teschke CM (2013) An intramolecular chaperone inserted in bacteriophage P22 coat protein mediates its chaperonin-independent folding. J Biol Chem 288:33772–33783. doi: 10.1074/jbc.M113.515312 CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media Dordrecht 2015

Authors and Affiliations

  1. 1.Department of Molecular & Cell Biology, and ChemistryUniversity of ConnecticutStorrsUSA
  2. 2.Department of Molecular, Microbial, and Structural BiologyUniversity of Connecticut HealthFarmingtonUSA
  3. 3.Department of ChemistryUniversity of ConnecticutStorrsUSA

Personalised recommendations