p-Hydroxybenzoate hydroxylase (PobA) is a possible drug target to combat tetracycline resistance. Here, the 2.2 Å resolution structure of PobA from the pathogen Pseudomonas putida complexed with FAD is reported and is compared with those of PobA from P. aeruginosa and P. fluorescens.

The structure of the Monkeypox virus protein A42R has been determined at a resolution of 1.52 Å. This protein has a backbone structure similar to that of cellular profilin, but structural variation in loop regions and a surface basic patch support biochemical data showing that this protein has distinct binding interactions with actin and phosphatidylinositol lipids and is not likely to bind proline-rich domain proteins or microtubules.

The structure of P. falciparum GAPDH has been solved to 2.6 Å resolution with one molecule of NAD⁺ bound per subunit. Amino-acid substitutions which cluster in a groove about the R dyad suggest a potential binding site for haem, which is known to specifically inhibit the Plasmodium enzyme.