pISSN 2288-6982
eISSN 2288-7105




BioDesign 2022; 10(2): 29-33

Published online June 30, 2022

© Korean Society for Structural Biology

NADH-dependent butanol dehydrogenase from Fusobacterium nucleatum: purification, crystallization, and X-ray crystallographic analysis

Xue Bai1,2,†, Jing Lan1,2,†, Shanru He1,2, Tingting Bu1,2, Jie Zhang1,2, Lulu Wang1,2, Chunshan Quan1,2, Ki Hyun Nam3, Nam-Chul Ha4,* and Yongbin Xu1,2,*

1Department of Bioengineering, College of Life Science, Dalian Minzu University, Dalian 116600, Liaoning, China
2Key Laboratory of Biotechnology and Bioresources Utilization, Ministry of Education, College of Life Science, Dalian Minzu University, Dalian 116600, Liaoning, China
3Department of Life Science, Pohang University of Science and Technology, Pohang 35398, Republic of Korea
4Department of Agricultural Biotechnology, College of Agriculture and Life Sciences, Seoul National University, Seoul 08826, Republic of Korea

Correspondence to: *,
These authors contributed equally to this work.

Received: March 16, 2022; Revised: April 8, 2022; Accepted: April 11, 2022


Fusobacterium nucleatum is a dangerous pathogen, and it has been linked to a variety of health problems, including cancer, periodontal disease, and pregnancy complications. F. nucleatum butanol dehydrogenase (FnYqdH) is a group of dehydrogenase enzymes that facilitate interconversion between butyraldehyde and butanol at the expenditure of a cofactor NAD (P)H. In this study, FnYqdH was successfully expressed and purified using Ni-NTA affinity, Q anionexchange, and gel-filtration chromatography. The protein crystal was obtained and diffracted to a resolution of 2.0 Å. The crystal belonged to the orthorhombic space group of I222, with unit-cell parameters of a = 64.77, b = 78.85, and c = 215.22 Å. The Matthews coefficient and solvent content were estimated to be 3.19 Å3 Da–1 and 61.49%, respectively, assuming that the asymmetric unit contained only one recombinant protein molecule. Size-exclusion chromatography suggested that FnYqdH prefers to exist as a dimer in the solution.