Complex structure of a bacterial class 2 histone deacetylase homologue with a trifluoromethylketone inhibitor
Histone deacetylases (HDACs) are involved in the regulation of gene expression and are thus attractive targets in the development of novel anticancer drugs. We have determined the crystal structure of a bacterial HDAC-like enzyme with bound trifl uoromethylketone inhibitor 9,9,9-trifluoro-8-oxo-
N-phenylnonanamide representing a novel type of nonhydroxamate inhibitor for HDACs. This structure not only reveals details of the inhibitor–enzyme interaction, but also provides hints on how to improve the inhibitor.
T.K. Nielsen, C. Hildmann, D. Riester, D. Wegener, A. Schwienhorst and R. Ficner
![[HDAC-like enzyme]](https://www.iucr.org/__data/assets/image/0006/4110/320ActaF.tif.gif)
Active site of the bacterial HDAC-like enzyme with bound 9,9,9-trifluoro-8-oxo-Nphenylnonanamide inhibitor. The inhibitor exhibits two conformations (colored yellow and cyan, respectively).
