Structural and biophysical characterization of the Borna disease virus 1 phosphoprotein

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.

Structures of chloramphenicol acetyltransferase III and Escherichia coli β-keto­acylsynthase III co-crystallized with partially hydrolysed acetyl-oxa(de­thia)CoA

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.

Expression, purification and crystallization of N-acetyl-(R)-β-phenylalanine acylases derived from Burkholderia sp. AJ110349 and Variovorax sp. AJ110348 and structure determination of the Burkholderia enzyme

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.