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Publication Abstract from PubMed

As an important bacterial second messenger, bis-(3',5')-cyclic diguanylate (cyclic di-GMP or c-di-GMP) has been implicated in numerous biological activities, including biofilm formation, motility, survival and virulence. These processes are manipulated by the binding of c-di-GMP to its receptors. XC_3703 from the plant pathogen Xanthomonas campestris pv. campestris, which belongs to the YajQ family of proteins, has recently been identified as a potential c-di-GMP receptor. XC_3703, together with XC_2801, functions as a transcription factor activating virulence-related genes, which can be reversed by the binding of c-di-GMP to XC_3703. However, the structural basis of how c-di-GMP regulates XC_3703 remains elusive. In this study, the structure of XC_3703 was determined to 2.1 A resolution using the molecular-replacement method. The structure of XC_3703 consists of two domains adopting the same topology, which is similar to that of the RNA-recognition motif (RRM). Arg65, which is conserved among the c-di-GMP-binding subfamily of the YajQ family of proteins, together with Phe80 in domain II, forms a putative c-di-GMP binding site.

Crystal structure of the YajQ-family protein XC_3703 from Xanthomonas campestris pv. campestris.,Zhao Z, Wu Z, Zhang J Acta Crystallogr F Struct Biol Commun. 2016 Sep;72(Pt 9):720-5. doi:, 10.1107/S2053230X16013017. Epub 2016 Aug 26. PMID:27599864^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.