Biochemical features of the novel Tail Tubular Protein A of Yersinia phage phiYeO3-12.

Scientific Reports
Anna PyraEwa Brzozowska

Abstract

Tail Tubular Protein A (TTPA) was long thought to be strictly a structural protein of environmental bacteriophages. However, our recent work has suggested that some TTPAs have additional functional features and thus are dual-function proteins. This study introduces a new TTPA family member, TTPAgp11, which belongs to Yersinia phage phiYeO3-12. We cloned the gene, expressed it and then purified the phage protein. The protein, including its hydrolytic activity, was characterized. Our enzymatic activity tests showed that TTPAgp11 displayed hydrolytic activity towards Red-starch, suggesting that this enzyme could be classified as part as the α - 1, 4-glucosidase family. Protein folding and aggregation tests indicated that TTPAgp11 is a single-domain protein whose aggregation can be induced by maltose or N-acetylglucosamine. The spatial structure of TTPAgp11 seemed to resemble that of the first reported dual-function TTPA, TTPAgp31, which was isolated from Klebsiella pneumoniae phage 32.

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Datasets Mentioned

BETA
AJ251805

Methods Mentioned

BETA
X-ray
circular dichroism
PCR

Software Mentioned

HHPred
BLAST
StabilityAnalysis
ThermControl
Bruker
PR
Clustal Omega
Phyre
Tasser

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