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BIO DESIGN

pISSN 2288-6982
eISSN 2288-7105

Article

Article

Crystallization

BioDesign 2021; 9(1): 19-22

Published online March 30, 2021

https://doi.org/10.34184/kssb.2021.9.1.19

© Korean Society for Structural Biology

Purification, crystallization, and preliminary X-ray analysis of a putative N-terminal acetyltransferase encoded by a Salmonellainfecting bacteriophage

Yongseong Hyun1, Nayeon Ki1, Nam-Chul Ha1,* and Hyun-Myung Oh2,*

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

Correspondence to: marinebio@pknu.ac.kr, hanc210@snu.ac.kr

Received: February 7, 2021; Revised: March 12, 2021; Accepted: March 16, 2021

Abstract

Bacteriophages infect host bacteria and control host metabolism through diverse mechanisms. We noted a gene harboring homology in the N-terminal acetyltransferase of a bacteriophage SPN3US, which infects Salmonella. The phage-encoded gene is phylogenetically remote from the typical N-terminal acetyltransferases whose structures are available. This study reports a preliminary analysis of the crystals of phage-encoded N-terminal acetyltransferase, including its purification and crystallization. The crystals diffracted X-rays to a 2.2 Å resolution, revealing that the crystals belong to P6122 or P6522 with unit cell parameters of a = 68.5 and c = 219.0 Å. We are now growing the selenomethionine-substituted crystals to obtain the phase information. The protein structure will provide molecular insights on how the phage hijacks the bacterial host metabolism.