issue contents

ISSN: 2053-230X

March 2023 issue

Highlighted illustration

Cover illustration: Borna disease virus 1 phosphoprotein [Whitehead et al. (2023), Acta Cryst. F79, 51–60]. Bornaviruses are RNA viruses which can infect neuronal cells and, in rare cases, cause a lethal encephalitis. Here, the oligomerization domain of a viral phosphoprotein that is required for the formation of a functional replication/transcription complex has been studied.

research communications

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The phosphoprotein is an essential component of the replication complex in bornaviruses. Here, using X-ray crystallography, the structure of the phosphoprotein from Borna disease virus 1 is presented and its flexibility in solution is characterized.

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Stable analogs of acetyl-CoA are needed to support structure–function studies of acetyltransferase enzymes. Here, the structures of two enzymes in the presence of an acetyl-CoA analog in which the thioester is replaced by an ester are reported.

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The structure of N-acetyl-(R)-β-phenylalanine acylase from Burkholderia sp. AJ110349 was determined. The three domains showed structural similarity to the corresponding domains of the large subunit of N,N-dimethylformamidase from Paracoccus sp. strain DMF, despite the quaternary structures of these holoenzymes in solution being completely different from each other.
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