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KMID : 0880220220600070746
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Journal of Microbiology
2022 Volume.60 No. 7 p.746 ~ p.755
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Crystal structure of the phage-encoded N-acetyltransferase in complex with acetyl-CoA, revealing a novel dimeric arrangement
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Ki Na-Yeon
Jo In-Seong
Hyun Yong-Seong
Lee Jin-Wook
Ha Nam-Chul
Oh Hyun-Myung
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Abstract
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Bacteriophages employ diverse mechanisms to facilitate the proliferation of bacteriophages. The Salmonella-infecting phage SPN3US contains a putative N-acetyltransferase, which is widely found in bacteriophages. However, due to low sequence similarity to the N-acetyltransferases from bacteria and eukaryotic cells, the structure and function of phage-encoded acetyltransferases are mainly unknown. This study determines the crystal structure of the putative N-acetyltransferase of SPN3US in complex with acetyl-CoA. The crystal structure showed a novel homodimeric arrangement stabilized by exchanging the C-terminal α-helix within the dimer. The following biochemical analyses suggested that the phage-encoded acetyltransferase might have a very narrow substrate specificity. Further studies are required to reveal the biochemical activity, which would help elucidate the interaction between the phage and host bacteria in controlling pathogenic bacteria.
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KEYWORD
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acetyl-CoA, Gcn5-related N-acetyltransferases (GNATs), Salmonella-infecting phage SPN3US
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