issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

March 2022 issue

Highlighted illustration

Cover illustration: Chlamydia trachomatis inorganic pyrophosphatase (CtPPase) [Maddy et al. (2022), Acta Cryst. F78, 135–142]. C. trachomatis is the leading cause of bacterial sexually transmitted infections and 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.

topical reviews


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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


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An electron-microscopy model of the SET3 histone deacetylase complex reveals a three-lobe architecture.

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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.

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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.

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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


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