Premium
Crystal structure of the ATPase‐C domain of the chromatin remodeller Fun30 from Saccharomyces cerevisiae
Author(s) -
Liu Lan,
Jiang Tao
Publication year - 2017
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x16019269
Subject(s) - chromatin , subfamily , atpase , saccharomyces cerevisiae , regulator , dna , gene silencing , crystal structure , microbiology and biotechnology , domain (mathematical analysis) , biology , gene , chemistry , genetics , biophysics , biochemistry , crystallography , enzyme , mathematical analysis , mathematics
Fun30 (Function unknown now 30) is a chromatin remodeller belonging to the Snf2 family. It has previously been reported to be a regulator of several cellular activities, including DNA repair, gene silencing and maintenance of chromatin structure. Here, the crystal structure of the Fun30 ATPase‐C domain (the C‐lobe of the ATPase domain) is reported at 1.95 Å resolution. Although the structure displays overall similarities to those of other Snf2 family members, a new structural module was found to be specific to the Fun30 subfamily. Fun30 ATPase‐C was shown be monomeric in solution and showed no detectable affinity for dsDNA.