issue contents
March 2022 issue
topical reviews
Open access
6-Phosphogluconate dehydrogenase is in a process of a continuous discovery: despite the determination of several crystal structures over thirty years, a clear elucidation of its mechanism from the structure–function point of view has not yet been reached.
research communications
An electron-microscopy model of the SET3 histone deacetylase complex reveals a three-lobe architecture.
BRD2 is a promising drug target for the treatment of various cancers. Crystal structures of BRD2 bromodomains BD1 and BD2 in complexes with a pyrano-1,3-oxazine derivative and phenanthridinone compounds were determined. Crystal structures and biochemical assays confirm that these ligands are indeed potent inhibitors of BRD2 bromodomains.
Open access
In bacteria, high-affinity zinc import is accomplished by ATP-binding cassette (ABC) transporters, which rely on extracellular solute-binding proteins (SBPs) to acquire the metal and deliver it to the membrane permease. The crystal structure of the zinc-bound (holo) form of Citrobacter koseri SBP ZnuA has been determined. Despite 95% sequence identity to the ZnuA homologue from Salmonella enterica, C. koseri ZnuA exhibits different zinc-coordination and a closed rather than open conformation. Comparison with other close ZnuA homologue structures suggests a flexible conformational landscape that may be important for zinc binding and/or delivery to the permease.
PDB reference: ZnuA from Citrobacter koseri, 7rcj
Open access
Chlamydia trachomatis is the leading cause of bacterial sexually transmitted infections. C. trachomatis inorganic pyrophosphatase (CtPPase) hydrolyzes inorganic pyrophosphate during metabolism. A 2.2 Å resolution X-ray structure of CtPPase reveals shared structural features that may facilitate the repurposing of inhibitors identified for bacterial inorganic pyrophosphatases as starting points for new therapeutics.
addenda and errata
Open access
The article by Beard et al. [(2022), Acta Cryst. F78, 59–65] is corrected.