5H5O

A cyclic-GMP-dependent signalling pathway regulates bacterial phytopathogenesis

「4KG1」から置き換えられました

5H5O の概要

• エントリーDOI: 10.2210/pdb5h5o/pdb
• 分子名称: Diguanylate cyclase, CYCLIC GUANOSINE MONOPHOSPHATE (3 entities in total)
• 機能のキーワード: cyclic gmp, xc0250, xc0249, signalling pathway, biosynthetic protein
• 由来する生物種: Xanthomonas campestris pv. campestris (strain B100)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 29688.00

構造登録者

Chin, K.H.,Chou, S.-H. (登録日: 2016-11-08, 公開日: 2017-05-24, 最終更新日: 2024-10-23)

主引用文献

An, S.Q.,Chin, K.H.,Febrer, M.,McCarthy, Y.,Yang, J.G.,Liu, C.L.,Swarbreck, D.,Rogers, J.,Maxwell Dow, J.,Chou, S.-H.,Ryan, R.P.
A cyclic GMP-dependent signalling pathway regulates bacterial phytopathogenesis
EMBO J., 32:2430-2438, 2013

PubMed Abstract: Cyclic guanosine 3',5'-monophosphate (cyclic GMP) is a second messenger whose role in bacterial signalling is poorly understood. A genetic screen in the plant pathogen Xanthomonas campestris (Xcc) identified that XC_0250, which encodes a protein with a class III nucleotidyl cyclase domain, is required for cyclic GMP synthesis. Purified XC_0250 was active in cyclic GMP synthesis in vitro. The linked gene XC_0249 encodes a protein with a cyclic mononucleotide-binding (cNMP) domain and a GGDEF diguanylate cyclase domain. The activity of XC_0249 in cyclic di-GMP synthesis was enhanced by addition of cyclic GMP. The isolated cNMP domain of XC_0249 bound cyclic GMP and a structure-function analysis, directed by determination of the crystal structure of the holo-complex, demonstrated the site of cyclic GMP binding that modulates cyclic di-GMP synthesis. Mutation of either XC_0250 or XC_0249 led to a reduced virulence to plants and reduced biofilm formation in vitro. These findings describe a regulatory pathway in which cyclic GMP regulates virulence and biofilm formation through interaction with a novel effector that directly links cyclic GMP and cyclic di-GMP signalling.

PubMed: 23881098
DOI: 10.1038/emboj.2013.165

実験手法

X-RAY DIFFRACTION (2.122 Å)