5B7W

Crystal structure of the YajQ-family protein XC_3703 from Xanthomonas campestris pv.campestris

Summary for 5B7W

• Entry DOI: 10.2210/pdb5b7w/pdb
• Descriptor: UPF0234 protein XC_3703 (2 entities in total)
• Functional Keywords: receptor, unknown function
• Biological source: Xanthomonas campestris pv. campestris (strain 8004)
• Total number of polymer chains: 2
• Total formula weight: 38603.89

Authors

Zhao, Z.,Wu, Z. (deposition date: 2016-06-10, release date: 2016-09-07, Last modification date: 2024-03-20)

Primary citation

Zhao, Z.,Wu, Z.,Zhang, J.
Crystal structure of the YajQ-family protein XC_3703 from Xanthomonas campestris pv. campestris
Acta Crystallogr.,Sect.F, 72:720-725, 2016

PubMed Abstract: 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.

PubMed: 27599864
DOI: 10.1107/S2053230X16013017

Experimental method

X-RAY DIFFRACTION (2.08 Å)