- Crystal structure of the phage-encoded N-acetyltransferase in complex with acetyl-CoA, revealing a novel dimeric arrangement
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Nayeon Ki , Inseong Jo , Yongseong Hyun , Jinwook Lee , Nam-Chul Ha , Hyun-Myung Oh
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J. Microbiol. 2022;60(7):746-755. Published online July 4, 2022
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DOI: https://doi.org/10.1007/s12275-022-2030-2
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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 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.
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Citations
Citations to this article as recorded by  - Characteristics of the smallest brucellaphage with strong lytic ability
Hongbaiyu Liu, Youhong Zhong, Zhihong Zhang, Kehong Xu, Chunpeng Mao, Qiuju Yang, Lihua Yang, Binbin Yu, Ying Long, Xinyu Qin, Liyuan Shi, Sheng Chang, Yuanying Shen, Peng Wang
Frontiers in Veterinary Science.2025;[Epub] CrossRef - Structural basis for Salmonella infection by two Microviridae phages
Wanlong Hu, Zhengjie Liu, Yuming Wei, Qucheng Bian, Weiqi Lan, Chongzheng Fan, Jiaoyang Song, Qianqian Sun, Xiaojie Zhang, Yuqing Liu, Yan Gao, Yibao Chen
Communications Biology.2025;[Epub] CrossRef - Posttranslational modifications in bacteria during phage infection
Hannelore Longin, Nand Broeckaert, Vera van Noort, Rob Lavigne, Hanne Hendrix
Current Opinion in Microbiology.2024; 77: 102425. CrossRef
- Crystal structure of the nuclease and capping domain of SbcD from Staphylococcus aureus
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Jinwook Lee , Inseong Jo , Jinsook Ahn , Seokho Hong , Soyeon Jeong , Aeran Kwon , Nam-Chul Ha
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J. Microbiol. 2021;59(6):584-589. Published online April 20, 2021
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DOI: https://doi.org/10.1007/s12275-021-1012-0
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Abstract
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The SbcCD complex is an essential component of the DNA
double-strand break (DSB) repair system in bacteria. The
bacterial SbcCD complex recognizes and cleaves the DNA
ends in DSBs by ATP-dependent endo- and exonuclease
activities as an early step of the DNA repair process. SbcD
consists of nuclease, capping, and helix-loop-helix domains.
Here, we present the crystal structure of a SbcD fragment from
Staphylococcus aureus, which contained nuclease and capping
domains, at a resolution of 2.9 Å. This structure shows
a dimeric assembly similar to that of the corresponding domains
of SbcD from Escherichia coli. The S. aureus SbcD fragment
exhibited endonuclease activities on supercoiled DNA
and exonuclease activity on linear and nicked DNA. This
study contributes to the understanding of the molecular basis
for how bacteria can resist sterilizing treatment, causing DNA
damage.
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Citations
Citations to this article as recorded by - A Cas12a Toolbox for Rapid and Flexible Group B Streptococcus Genomic Editing and CRISPRi
G. H. Hillebrand, S. C. Carlin, E. J. Giacobe, H. A. Stephenson, J. Collins, T. A. Hooven
Molecular Microbiology.2025; 124(5): 449. CrossRef - Solvent-polarity-programmed chirality transfer in stereodiversified dipeptide-based self-assembly system with light-responsive circular dichroism property
Minghao Wang, Hanting Wang, Shunjie Cheng, Yuanyuan Wang, Lukang Ji
Colloids and Surfaces A: Physicochemical and Engineering Aspects.2025; 726: 137897. CrossRef - Molecular characterisation of Toxoplasma gondii Mre11 reveals unique structural features and potential as a therapeutic target
Diego M. Ruiz, Valeria R. Turowski, William J. Sullivan, Sergio O. Angel
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Kaiying Cheng, Yukang Sun, Huan Yu, Yingxuan Hu, Yini He, Yuanyuan Shen
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