Issues

In this issue Oldham and colleagues (pp. 57–74) have performed extensive structural and kinetic characterization of the SAT enzyme from the antibiotic-resistant pathogen Neisseria gonorrhoeae. Using X-ray crystallography, we have solved the structures of NgSAT with the non-natural ligand, l-malate. They present data which could be explored to combat the rise of antimicrobial resistant N. gonorrhoeae. The cover image shows a ribbon diagram of the NgSAT trimer illustrating the position and formation of the active site between two adjacent monomers. The image is courtesy of Joanna Hicks.