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Yongseong Hyun,기나연,하남출,오현명 한국구조생물학회 2021 Biodesign Vol.9 No.1
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.
Yongseong Hyun,Jinsook Ahn,Yeongjin Baek,Yongbin Xu,Nam-Chul Ha 한국구조생물학회 2020 Biodesign Vol.8 No.3
Brucella abortus is an intracellular bacterial pathogen that causes brucellosis in humans and livestock. The genome of B. abortus encodes the VirB type IV secretion system (T4SS), which is essential to its virulence. B. abortus produces and secretes effector proteins through the T4SS to survive in the intracellular environment and manipulate host immunity. The T4SS spans the peptidoglycan layer through vacancies in the peptidoglycan chain. Recently, secretion activator gene A (SagA) from B. abortus was identified as a lysozyme-like enzyme that creates holes in the peptidoglycan layer. In this study, SagA from B. abortus was overexpressed, purified, and crystallized. Crystal diffraction data were acquired at 2.0 Å resolution, a P213 space group with a unit cell parameter of 79.04 Å. We are currently exploring the crystal structure of SagA using the anomalous signal from selenomethionine-substituted crystals and an X-ray free-electron laser.