Crystal structure of TchmY from Actinoplanes teichomyceticus

The structural analysis of a putative prenylcyclase enzyme, TchmY, from Actinoplanes teichomyceticus is reported.

Structure of the archaeal chemotaxis protein CheY in a domain-swapped dimeric conformation

Che proteins are part of the signal transduction pathway between stimulus and response, mediated by the archaellum. The structure of the chemotaxis protein CheY was determined in two different crystal forms. The novel CheF protein that connects chemotaxis signaling to the motility apparatus was expressed and crystallized, and data were acquired by X-ray diffraction.

Structure of GTP cyclo­hydrolase I from Listeria monocytogenes, a potential anti-infective drug target

GTP cyclohydrolase I from Listeria monocytogenes, a putative anti-infective drug target, has been crystallized and the crystal structure was solved at 2.4 Å resolution.

No magnesium is needed for binding of the stimulator of interferon genes to cyclic dinucleotides

Stimulator of interferon genes (STING) is a key component of innate intracellular immunity. It is activated by the binding of cyclic dinucleotides (CDNs) produced by cyclic GMP-AMP synthase or of bacterial origin. The interactions of CDNs with STING are well understood; however, contrary to the previously published structure, it is shown that no Mg atoms are present in the binding site of STING.

Structural basis for the substrate recognition of aminoglycoside 7′′-phosphotransferase-Ia from Streptomyces hygroscopicus

The crystal structure of aminoglycoside 7′′-phosphotransferase-Ia from Streptomyces hygroscopicus in complex with hygromycin B has been determined at 2.4 Å resolution.

Crystal structure of UDP-glucose pyro­phosphorylase from Yersinia pestis, a potential therapeutic target against plague

The crystal structure of UDP-glucose pyrophosphorylase from Yersinia pestis has been determined to 2.17 Å resolution, providing a foundation for future structure-based drug-design studies.

Structure of the di­hydrolipo­amide succinyltransferase catalytic domain from Escherichia coli in a novel crystal form: a tale of a common protein crystallization contaminant

Dihydrolipoamide succinyltransferase, a protein crystallization contaminant, was crystallized in a new crystal form in space group I4 and its structure was determined.