issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

March 2018 issue

Highlighted illustration

Cover illustration: The HIV integrase-binding domain (IBD) of lens epithelium-derived growth factor (Hannon et al., p. 143). Drugs designed to interfere with protein-protein interactions involving IBD could be important for therapy in both AIDS and leukaemias.

research communications


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A crystallographic structure of native influenza A PB2cap was solved to 1.52 Å resolution. B-­factor difference plots and r.m.s.d. plots among known structures suggest functionally relevant disassociation of the N-terminal ligand-binding domain from the C-terminal domain.

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The crystallization of the YopT-like predicted cysteine protease domain of the secreted toxin PfhB2 from Pasteurella multocida (PfhB2-YopT) is reported. Sequence alignment with structures deposited in the Protein Data Bank indicated no reported homologous structures, suggesting that PfhB2-YopT may represent a novel putative cysteine protease.

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This paper is the first to describe the crystal structure of manganese superoxide dismutase from the genus Staphylococcus. Staphylococcus equorum and Bacillus subtilis MnSODs display different thermal and chemical stabilities. The slightly different structure of S. equorum MnSOD may provide an explanation for the differences in stability.

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The HIV integrase-binding domain (IBD) of lens epithelium-derived growth factor has been cloned, purified and crystallized, and its structure has been solved. IBD forms an unusual domain-swapped dimer that assembles into octamers in the crystal.

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Mouse claudin-3 was crystallized in complex with the carboxyl-terminal region of C. perfringens enterotoxin and a data set was collected to 4.2 Å resolution.

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The structure of MAPK-interacting kinase 1 (Mnk1) in complex with a novel Mnk1-selective inhibitor was determined. It was found that the inhibitor stabilizes the auto-inhibited inactive state of Mnk1.

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A putative phosphoribosyl transferase from phage BTCU-1 that infects Mycobacterium and shows no sequence similarity to any structure deposited in the Protein Data Bank was cloned, expressed, purified and crystallized. The crystals diffracted X-rays to 2.2 Å resolution.

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This article reports the crystal structure of MSMEG_4306, a hypothetical protein from Mycobacterium smegmatis, determined by zinc SAD phasing.

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NS1-binding protein (NS1-BP) is involved in many cell functions, including pre-mRNA splicing, the ERK signalling pathway, the aryl hydrocarbon receptor pathway, F-actin organization and protein ubiquitylation. Here, the structure of the C-terminal Kelch domain of NS1-BP is reported at 1.98 Å resolution.

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An ancestral bacterial pyruvate decarboxylase (with an inferred age of 1248 million years) was reconstructed through ancestral sequence reconstruction, synthesized and recombinantly expressed in E. coli. The enzyme is fully functional and its crystal structure was elucidated to 3.5 Å resolution.
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