issue contents

ISSN: 2053-230X

December 2018 issue

Highlighted illustration

Cover illustration: Protein phosphatase 1 (PP1) dephosphorylates hundreds of key biological targets by associating with nearly 200 regulatory proteins to form highly specific holoenzymes. Here the structure of an ancient highly conserved regulatory protein, SDS22, provides insights into the mechanism of heterodimer formation with PP1 [Choy et al. (2018), Acta Cryst. F74, 817-824].

research communications

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Large single crystals of the alcohol dehydrogenase from Lactobacillus brevis were generated, thus enabling neutron diffraction experiments to be performed for the first time with this protein. The obtained neutron structure revealed new details of the hydrogen-bonding network and provided new insights into the reasons why divalent magnesium or manganese ions are necessary for its activity.

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The inhibition of undecaprenyl pyrophosphate synthase (UPPS) may be an effective strategy in combating the multidrug-resistant pathogen Acinetobacter baumannii. The structure of UPPS from A. baumannii reported here may provide a structural basis for inhibitor design.

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The catalytic domain of α-1,3-glucanase FH1 from Paenibacillus glycanilyticus FH11, which may be of application in dental care and the development of fungal cell-wall lytic enzymes, was expressed and purified, and the protein was crystallized using the sitting-drop vapor-diffusion method. Diffraction data were collected to a resolution of 1.6 Å.

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The crystal structure of a dimethylsulfide monooxygenase from Hyphomicrobium sulfonivorans has been solved, and comparison with its structural homologues revealed that it has a different substrate-binding pocket.

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The glycoside hydrolase family 3 β-glucosidase Cel3A from Neurospora crassa (NcCel3A) is highly specific for cellobiose. The crystal structure of NcCel3A has been solved to 2.25 Å resolution. The structure is a dimer and exhibits a high degree of N-glycosylation.

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This paper describes the construction of a low-cost, open-source system for imaging the contents of multi-well plates.

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The crystal structure of Mycobacterium tuberculosis high-temperature requirement A (HtrA) protein reveals a conformational arrangement that is consistent with regulated catalytic activity. The structural data thus suggest that unlike other HtrA paralogues, this essential membrane-associated protease is unlikely to be constitutively active to perform housekeeping functions.

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The crystal structure of the type VI effector–immunity (Tae4–Tai4) complex from Agrobacterium tumefaciens is reported. A structural comparison with homologs revealed similarities and differences in the catalytic and inhibitory mechanisms among the Tae4 and Tai4 family proteins.

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SDS22 is an ancient protein phosphatase 1 (PP1) regulatory protein that associates with PP1 at kinetochores and regulates PP1-mediated dephosphorylation of Aurora B kinase. Here, the crystal structure of human SDS22 in a P212121 crystal form reveals that this leucine-rich repeat protein is highly curved, resulting in distinct surfaces that are likely to be important for PP1 binding.
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