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4 NAC domain, the one of A. thaliana ANAC019 (Ernst et al, 2004, EMBO Rep, 5:297-303), revealing a novel dimeric transcription factor fold. The structure is now the basis for mutagenesis studies to identify the DNA-binding mode (Olsen et al, 2005, Plant Science 169: 785-797) Structure determination of a new crystal form of this NAC domain shows that the dimer is likely to have some flexibility, but the solution structure as determined by small angle X-ray scattering is in good agreement with the original crystal structure. Based on ongoing crystallographic, small angle scattering and mutagenesis studies, our current model for NAC proteins binding to DNA will be presented.

Structure of the topoisomerase IV fromS. pneumoniaewith a DNA target and quinolone drug