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COVER: Structure of the antibiotic thiolactomycin (purple) bound at the active site of -ketoacyl-acyl carrier protein synthase I (FabB) superimposed over a scanning electron micrograph of Escherichia coli. Thiolactomycin forms strong hydrogen bond interactions with the two active site histidines (red dots) to block the activity of FabB, an elongation condensing enzyme in bacterial fatty acid biosynthesis. The use of computational and structural analysis in the investigation of proteinprotein interactions and antibacterial drug discovery in type II fatty acid synthase systems is reviewed by Zhang et al. in this issue.

The cover illustration was designed by K. G. Murti and K. Barnes of the Scientific Imaging resource at St. Jude Children's Research Hospital, Memphis, TN. (See Zhang et al., p.1.)
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