issue contents

ISSN: 2053-230X

November 2016 issue

Highlighted illustration

Cover illustration: Crystal structure of a yeast 14-3-3 protein from Lachancea thermotolerans bound to a human lipid kinase PI4KB-derived peptide (Eisenreichova et al., p. 799).

research communications

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Crystal structures of a 14-3-3 protein (Bmh1) from the yeast L. thermotolerans in the unliganded form and in complex with a peptide from a human homologue (PI4KB) of its binding partner Pik1 reveal the high evolutionary conservation of 14-3-3 proteins. Indeed, the yeast 14-3-3 protein binds its human-derived ligand in a manner highly similar to that of human 14-3-3 proteins.

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The crystal structure of a phosphoribosyl anthranilate isomerase from the hyperthermophilic archaeon T. kodakaraensis was determined in space groups P1 and C2 at 1.75 and 1.85 Å resolution, respectively.

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The crystal structure of a triazolylthioacetamide inhibitor in complex with Verona integron-encoded metallo-β-lactamase 2 (VIM-2) is reported at a resolution of 1.50 Å. The structure shows that the inhibitor binds to the active site of the enzyme and reveals detailed information on the inhibitor interactions.

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The 1.34 Å resolution crystal structure of fuculose aldolase from the psychrophilic yeast G. antarctica reveals characteristics of the enzymatic site and tolerance to cold temperature.

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Active JAK1 kinase domain was crystallized with MgADP and soaked in the presence of EDTA to allow displacement of the nucleotide by compounds of interest. This high-throughput method of structure determination may be widely applicable to other protein kinases and small-molecule ATP-competitive ligands.

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B. japonicum D-sorbitol dehydrogenase is NADH-dependent. It is of interest for industrial applications because of its ability to also oxidize L-glucitol and its thermostability. Here, its structure is presented and discussed.
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