issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

September 2019 issue

Highlighted illustration

Cover illustration: A potential anti-infective drug target, GTP cyclohydrolase I from Listeria monocytogenes [Schüssler et al. (2019), Acta Cryst. F75, 586-592].

research communications


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

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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.

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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.

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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.

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

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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.

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