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

作者：Tripler Therese N; Maciejewski Mark W; Teschke Carolyn M^*; Alexandrescu Andrei T

来源：Biomolecular NMR Assignments, 2015, 9(2): 333-336.

DOI：10.1007/s12104-015-9604-4

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

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 beta-barrel, has been shown to govern the assembly, stability and size of the resulting capsid particles. Here, we report the H-1, N-15, and C-13 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.

• 出版日期2015-10