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Crystal structure of the YajQ‐family protein XC_3703 from Xanthomonas campestris pv. campestris
Author(s) -
Zhao Zhixin,
Wu Zhen,
Zhang Jun
Publication year - 2016
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x16013017
Subject(s) - xanthomonas campestris , subfamily , chemistry , biology , gene , biochemistry
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 Å 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.