| Title | Crystal structure of the phage-encoded N-acetyltransferase in complex with acetyl-CoA, revealing a novel dimeric arrangement |
|---|---|
| Author | Nayeon Ki1,2,3, Inseong Jo1,2,3, Yongseong Hyun1,2,3, Jinwook Lee1,2,3, Nam-Chul Ha1,2,3*, and Hyun-Myung Oh4* |
| Address | 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 Korea |
| Bibliography | Journal of Microbiology, 60(7),746-755, 2022, |
| DOI | 10.1007/s12275-022-2030-2 |
| Key Words | acetyl-CoA, Gcn5-related N-acetyltransferases (GNATs), Salmonella-infecting phage SPN3US |
| 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. |