Crystal Structure of the DNA-binding Domain of the LysR-type Transcriptional Regulator CbnR in Complex with a DNA Fragment of the Recognition-binding Site

Abstract

LysR-type transcriptional regulators（LTTRs）are one of the most abundant transcriptional regulators in bacteria. CbnR derived from Cupriavidus necator NH9 is an LTTR involved in transcriptional activation of the cbnABCD genes that encode chlorocatechol degradative enzymes. The crystal structure of the DNA binding domain of CbnR（CbnR_DBD）in complex with recognition binding site（RBS）of the cbnA promoter showed details of interaction between the CbnR_DBD and RBS. We analyzed the sequence selectivity of CbnR by comparison of the CbnR_DBD-RBS and the BenM_DBD-RBS complexes.