Open AccessCrystallization and preliminary X‐ray crystallographic analysis of human FAF1 UBX domain
Author(s) -
Kang Wonchull,
Shin Hwa Young,
Yang Jin Kuk
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110001077
Subject(s) - ultrabithorax , ubiquitin , crystallography , proteasome , crystallization , microbiology and biotechnology , biophysics , chemistry , biology , biochemistry , mutant , gene , homeotic gene , organic chemistry
Fas‐associated factor 1 (FAF1) is a multifunctional pro‐apoptotic protein that is involved in Fas‐mediated apoptosis, NF‐κB signalling and the ubiquitin–proteasome pathway. In the ubiquitin–proteasome pathway, FAF1 binds to the N domain of p97/VCP, a molecular chaperone that acts in complex with the proteasome, through its C‐terminal UBX domain and inhibits the proteasomal protein‐degradation process. In an effort to elucidate the structural basis of the function of FAF1 in modulating p97/VCP activity related to proteasomal protein degradation, crystallographic analysis of the FAF1 UBX domain and the p97/VCP N domain was initiated. Following the recently reported crystallization of the FAF1 UBX domain bound to the p97/VCP N domain, the unbound FAF1 UBX domain was also crystallized for purposes of structural comparison. X‐ray data were collected to 3.00 Å resolution and the crystals belonged to space group F 4 1 32, with unit‐cell parameters a = b = c = 176.40 Å. The Matthews coefficient and solvent content were estimated to be 3.04 Å 3 Da −1 and 59.5%, respectively, assuming that the asymmetric unit contained two molecules of the UBX domain, which was subsequently confirmed by molecular‐replacement calculations.