Purification, crystallization, and preliminary analysis of the lysozyme-like enzyme SagA from Brucella abortus

• 발행기관: 한국구조생물학회
• 저자명: Yongseong Hyun Jinsook Ahn Yeongjin Baek Yongbin Xu Nam-Chul Ha
• 간행물 정보: 『Biodesign』Vol 8, No 3, Sep, 64~67쪽, 전체 4쪽
• 주제분류: 자연과학 > 생물학
• 파일형태: PDF
• 발행일자: 2020.09.30

영문 초록

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.

목차

INTRODUCTION

RESULTS AND DISCUSSION

MATERIALS AND METHODS

ACKNOWLEDGEMENTS

REFERENCES