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.
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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.
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The authors declare no conflict of interest.
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Tripler, T.N., Maciejewski, M.W., Teschke, C.M. et al. NMR assignments for the insertion domain of bacteriophage CUS-3 coat protein. Biomol NMR Assign 9, 333–336 (2015). https://doi.org/10.1007/s12104-015-9604-4
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DOI: https://doi.org/10.1007/s12104-015-9604-4