Chemical biology: casting iron


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_Nature Chem. Biol._ doi:10.1038/nchembio.145 (2009) Bacteria use two biosynthetic pathways to create iron-scavenging molecules, called siderophores, that are essential to their


proliferation. Most siderophore research has focused on one of these — the nonribosomal peptide synthetase (NRPS)-dependent pathway — whereas the other, the NRPS-independent siderophore


(NIS) pathway, has been largely ignored. James Naismith of the University of St Andrews in Scotland and his colleagues are the first to solve a NIS enzyme's structure: that of AcsD,


which occurs in the plant pathogen _Pectobacterium chrysanthemi_. The structure reveals that AcsD catalyses reactions between ATP, citric acid and an amino acid, l-serine, making a probable


precursor to the siderophore. The authors hope their work will help in the design of inhibitors of siderophore-making enzymes from human pathogens. RIGHTS AND PERMISSIONS Reprints and


permissions ABOUT THIS ARTICLE CITE THIS ARTICLE Chemical biology: Casting iron. _Nature_ 457, 638 (2009). https://doi.org/10.1038/457638e Download citation * Published: 04 February 2009 *


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