Cover caption: Three-dimensional structure of the cell division inhibitor MinC from Thermotoga maritima (Protein Data Bank file 1HF2). Each monomer comprises an FtsZ-interacting domain (magenta/pink) and a MinD-interacting domain (orange/yellow) separated by a short flexible linker (red). The MinD-interacting domain is also responsible for MinC dimerization. The T. maritima structure appears to be a good model for the Escherichia coli protein, despite limited sequence similarity. (See related article on page 6684.)

© 2001, American Society for Microbiology