학술논문
Crystal structure of the putative HOCl and HOSCN-responsive peroxiredoxin RclX from Pseudomonas aeruginosa
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- 영문명
- Crystal structure of the putative HOCl and HOSCN-responsive peroxiredoxin RclX from Pseudomonas aeruginosa
- 발행기관
- 한국구조생물학회
- 저자명
- Nayeon Ki Jiheon Kim Doyeon Kim Inseong Jo
- 간행물 정보
- 『Biodesign』Vol 11, No 3, Sep, 39~44쪽, 전체 6쪽
- 주제분류
- 자연과학 > 생물학
- 파일형태
- 발행일자
- 2023.09.30
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국문 초록
영문 초록
Pseudomonas aeruginosa is an opportunistic pathogen that often evades eradication by the host immune response, particularly in immunocompromised individuals. Host immune cells produce various antimicrobial oxidants, including H2O2, HOCl, and HOSCN. Recently, a putative peroxiredoxin, RclX, was identified in P. aeruginosa as a highly upregulated gene in response to HOCl and HOSCN. However, the mechanism by which RclX scavenges HOCl and HOSCN stress remains unclear. In this study, we determined the crystal structure of RclX in homohexameric form. The overall structure of RclX closely resembled that of lpg0406, a carboxymuconolactone decarboxylase (CMD) family member from Legionella pneumophila. We found a hydrogen peroxide molecule near the substrate binding pocket, and the conserved CXXC motifs formed disulfide bond bridges in the crystal structure. Our findings provide structural insights into how P. aeruginosa exhibits high resistance to HOCl and HOSCN during host immune responses, with implications for eradicating persistent P. aeruginosa infections.
목차
INTRODUCTION
METHODS AND MATERIALS
RESULTS
DISCUSSION
ACKNOWLEDGEMENTS
CONFLICT OF INTEREST
REFERENCES
키워드
해당간행물 수록 논문
- Fusobacterium nucleatum FabG 3-ketoacyl-acyl carrier protein reductase: purification, crystallization, and X-ray crystallographic analysis
- Candida auris Aldo-keto reductase AldO: purification, crystallization, and X-ray crystallographic analysis
- Crystal structure of the putative HOCl and HOSCN-responsive peroxiredoxin RclX from Pseudomonas aeruginosa
- Cryo-electron tomography: a triumphant breakthrough in structural biology
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