issue contents
August 2023 issue

Cover illustration: Crystal structure of Prp16 in complex with ADP [Garbers et al. (2023), Acta Cryst. F79, 200–207]. The DEAH-box helicase Prp16 plays a crucial role in pre-mRNA splicing and is the driving force during spliceosomal catalysis. Here, the first crystal structure of Prp16 from Chaetomium thermophilum in complex with ADP is reported at 1.9 Å resolution.
research communications
Prp16 is a DEAH-box ATPase required for the splicing of pre-mRNA. The X-ray crystal structure of the Prp16-ADP complex was determined at a resolution of 1.9 Å.
The crystal structure of M. tuberculosis FadD23 complexed with the inhibitor 5′-O-[N-(11-phenoxyundecanoyl)sulfamoyl]adenosine was solved at 2.64 Å resolution and compared with similar three-dimensional structures. It is proposed that the inhibitor blocks substrate transfer from FadD23 to polyketide synthase 2.
The 3D structure of a GCN5-related N-acetyltransferase enzyme that is selective for canavanine has been elucidated and shown to share the fold and catalytic mechanism of the polyamine acetyltransferase subclass.