Dataset for: Structural insights into repression of <i>Pneumococcal</i> fatty acid synthesis pathway via repressor FabT and co-repressor acyl-ACP

Streptococcus pneumoniae fatty acid synthesis pathway is globally controlled at the transcriptional level by repressor FabT and co-repressor acyl-ACP, the intermediate of phospholipid synthesis. Here we report the crystal structure of FabT complexed with a 23-bp dsDNA, indicating that FabT is a weak repressor of low DNA-binding affinity in the absence of acyl-ACP. Modification of ACP with a long-chain fatty acid is necessary for the formation of a stable complex with FabT, mimicking in vitro by cross-linking, which would significantly elevate the DNA-binding affinity of FabT. Altogether, we propose a putative working model of gene repression under the double controls of FabT and acyl-ACP, elucidating a distinct repression network for Pneumococcus to precisely coordinate fatty acid synthesis.