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4 citations found for Satchell, J.
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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.
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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.
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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.