C4-dicarboxylates sensing mechanism revealed by the crystal structures of DctB sensor domain. Academic Article uri icon


  • C(4)-dicarboxylates are the major carbon and energy sources during the symbiotic growth of rhizobia. Responses to C(4)-dicarboxylates depend on typical two-component systems (TCS) consisting of a transmembrane sensor histidine kinase and a cytoplasmic response regulator. The DctB-DctD system is the first identified TCS for C(4)-dicarboxylates sensing. Direct ligand binding to the sensor domain of DctB is believed to be the first step of the sensing events. In this report, the water-soluble periplasmic sensor domain of Sinorhizobium meliloti DctB (DctBp) was studied, and three crystal structures were solved: the apo protein, a complex with C(4) succinate, and a complex with C(3) malonate. Different from the two structurally known CitA family of carboxylate sensor proteins CitA and DcuS, the structure of DctBp consists of two tandem Per-Arnt-Sim (PAS) domains and one N-terminal helical region. Only the membrane-distal PAS domain was found to bind the ligands, whereas the proximal PAS domain was empty. Comparison of DctB, CitA, and DcuS suggests a detailed stereochemistry of C(4)-dicarboxylates ligand perception. The structures of the different ligand binding states of DctBp also revealed a series of conformational changes initiated upon ligand binding and propagated to the N-terminal domain responsible for dimerization, providing insights into understanding the detailed mechanism of the signal transduction of TCS histidine kinases.

published proceedings

  • J Mol Biol

author list (cited authors)

  • Zhou, Y., Nan, B., Nan, J., Ma, Q., Panjikar, S., Liang, Y., Wang, Y., & Su, X.

citation count

  • 68

complete list of authors

  • Zhou, Yan-Feng||Nan, Beiyan||Nan, Jie||Ma, Qingjun||Panjikar, Santosh||Liang, Yu-He||Wang, Yiping||Su, Xiao-Dong

publication date

  • October 2008