Abstract

Article info Vol. 7  No. 2   pp.  38 ~ 41
Title Purification, crystallization, and X-ray crystallographic analysis of fatty acid amide hydrolase from Candida albicans
Authors Cho-Ah Min1, Ji-Sook Yun1, Je-Hyun Yoon2 and Jeong Ho Chang1,*
Institutions 1Department of Biology Education, Kyungpook National University, Daegu 41566, Republic of Korea, 2Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC 29425, USA *Correspondence: jhcbio@knu.ac.kr
Abstract Fatty acid amide hydrolase (FAAH) is a member of the amidase signature (AS) family of serine hydrolases. FAAH hydrolyzes anandamide and oleamide, which regulate pain perception, inflammation, and the cognitive state. Thus far, a limited number of structures of mammalian FAAH and non-mammalian AS family members have been determined. In this study, to understand structural features and functional diversity of FAAH, we crystallized the FAAH protein from the pathogenic fungus Candida albicans. X-ray diffraction data were obtained at 2.2 Å resolution. The crystal of the C. albicans FAAH (CaFAAH) belonged to P21, with the unit cell parameters a = 84.8, b = 68.7, c = 100.9 Å, α = γ = 90, and β = 99.6°. The crystals contained two CaFAAH molecules in asymmetric units.