Crystal structure of the phage-encoded N-acetyltransferase in complex with acetyl-CoA, revealing a novel dimeric arrangement

Nayeon Ki; Inseong Jo; Yongseong Hyun; Jinwook Lee; Nam-Chul Ha; Hyun-Myung Oh

doi:10.1007/s12275-022-2030-2

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Crystal structure of the phage-encoded N-acetyltransferase in complex with acetyl-CoA, revealing a novel dimeric arrangement: Nayeon Ki ^1,2,3, Inseong Jo ^1,2,3, Yongseong Hyun ^1,2,3, Jinwook Lee ^1,2,3, Nam-Chul Ha ^1,2,3, Hyun-Myung Oh ⁴; Journal of Microbiology 2022;60(7):746-755
DOI: https://doi.org/10.1007/s12275-022-2030-2
Published online: July 4, 2022

¹Research Institute of Agriculture and Life Sciences, CALS, Seoul National University, Seoul 08826, Republic of Korea, ²Center for Food and Bioconvergence, CALS, Seoul National University, Seoul 08826, Republic of Korea, ³Department of Agricultural Biotechnology, CALS, Seoul National University, Seoul 08826, Republic of Korea, ⁴Institute of Liberal Arts Education, Pukyong National University, Busan 48547, Republic of Korea¹Research Institute of Agriculture and Life Sciences, CALS, Seoul National University, Seoul 08826, Republic of Korea, ²Center for Food and Bioconvergence, CALS, Seoul National University, Seoul 08826, Republic of Korea, ³Department of Agricultural Biotechnology, CALS, Seoul National University, Seoul 08826, Republic of Korea, ⁴Institute of Liberal Arts Education, Pukyong National University, Busan 48547, Republic of Korea

Corresponding author: Nam-Chul Ha , Tel: +82-02-880-4853;,
Hyun-Myung Oh , Tel: +82-02-880-4853;,

Received: 27 January 2022 • Revised: 29 April 2022 • Accepted: 31 May 2022

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Abstract

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 phageencoded 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.

Keywords: Biosynthesis;Heterologous expression;Lanthipeptide;Lipolanthine

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Crystal structure of the phage-encoded N-acetyltransferase in complex with acetyl-CoA, revealing a novel dimeric arrangement

J. Microbiol. 2022;60(7):746-755. Published online July 4, 2022

DOI: https://doi.org/10.1007/s12275-022-2030-2

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