Fusobacterium nucleatum FabG 3-ketoacyl-acyl carrier protein reductase: purification, crystallization, and X-ray crystallographic analysis

• 영문명: Fusobacterium nucleatum FabG 3-ketoacyl-acyl carrier protein reductase: purification, crystallization, and X-ray crystallographic analysis
• 발행기관: 한국구조생물학회
• 저자명: Shanru He Yongbin Xu
• 간행물 정보: 『Biodesign』Vol 11, No 3, Sep, 50~54쪽, 전체 5쪽
• 주제분류: 자연과학 > 생물학
• 파일형태: PDF
• 발행일자: 2023.09.30

영문 초록

3-ketoacyl-acyl carrier protein (ACP) reductase is a vital enzyme in the biosynthesis of fatty acids in bacteria and plants. It assumes a critical role in the elongation process of fatty acids. The enzyme’s primary function is to catalyze the reduction of a 3-ketoacyl-ACP intermediate, forming a fully saturated acyl-ACP. This saturated acyl-ACP can subsequently elongate within the fatty acid synthesis pathway. This study successfully expressed and purified FnFabG from Fusobacterium nucleatum using Ni-NTA affinity and gel-filtration chromatography. The protein crystal was obtained and diffracted to a resolution of 2.7 Å. The preliminary crystallographic analysis suggested that FnFabG crystal belongs to the monoclinic space group P41212 with a = b = 111.56 Å and c = 88.69 Å, α = β = γ = 90.00°. The asymmetric unit contained one molecule of FnFabG, giving a solvent content of 78.33%.

목차

INTRODUCTION

RESULTS AND DISCUSSION

METHODS

ACKNOWLEDGEMENTS

CONFLICT OF INTEREST

REFERENCES