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November 2022 issue
Cover illustration: Ibuprofen – a common nonsteroidal anti-inflammatory drug – in complex with the zinc metalloenzyme human carbonic anhydrase II (hCA II). The hCA II inhibition profiles of ibuprofen and other carboxylic acid-based compounds are also presented and discussed in the article by Combs et al. [(2022), Acta Cryst. F78, 395–402].
research communications
The crystal structure of CapG from Staphylococcus aureus (SaCapG) forms a homohexamer, in contrast to the dimeric or tetrameric assembly of its bacterial homologues. The conformational flexibility of α2, the α2–α3 loop and α10 of SaCapG probably facilitates the binding of substrates and/or the release of products.
PDB reference: CapG from Staphylococcus aureus, 7ya2
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Three crystal forms of the type III secretion system export-gate protein SctV from two bacterial species reveal different cyclic oligomers, namely an octamer, a nonamer and a decamer.
The X-ray crystal structure of ibuprofen (a common nonsteroidal anti-inflammatory drug) in complex with the zinc metalloenzyme human carbonic anhydrase II (hCA II) is reported. In addition, the hCA II inhibition profiles of ibuprofen and other carboxylic acid-based compounds are presented and discussed.
PDB reference: carbonic anhydrase II in complex with ibuprofen, 8dj9
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