Summary for 5H5O
| Entry DOI | 10.2210/pdb5h5o/pdb |
| Descriptor | Diguanylate cyclase, CYCLIC GUANOSINE MONOPHOSPHATE (3 entities in total) |
| Functional Keywords | cyclic gmp, xc0250, xc0249, signalling pathway, biosynthetic protein |
| Biological source | Xanthomonas campestris pv. campestris (strain B100) |
| Total number of polymer chains | 2 |
| Total formula weight | 29688.00 |
| Authors | Chin, K.H.,Chou, S.-H. (deposition date: 2016-11-08, release date: 2017-05-24, Last modification date: 2024-10-23) |
| Primary citation | 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 Cited by 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: 23881098DOI: 10.1038/emboj.2013.165 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.122 Å) |
Structure validation
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