6JQA
Crystal structure of phyllogen, a phyllody inducing effector protein of phytoplasma.
Summary for 6JQA
| Entry DOI | 10.2210/pdb6jqa/pdb |
| Descriptor | Phytoplasmal effector causing phyllody 1, IODIDE ION, ... (5 entities in total) |
| Functional Keywords | phytoplasma, phyllody, phyllogen, phyl1, mads-domain transcription factor, transcription |
| Biological source | Onion yellows phytoplasma OY-W More |
| Total number of polymer chains | 4 |
| Total formula weight | 47471.14 |
| Authors | Miyatake, H.,Maejima, K. (deposition date: 2019-03-29, release date: 2019-05-15, Last modification date: 2024-11-06) |
| Primary citation | Iwabuchi, N.,Maejima, K.,Kitazawa, Y.,Miyatake, H.,Nishikawa, M.,Tokuda, R.,Koinuma, H.,Miyazaki, A.,Nijo, T.,Oshima, K.,Yamaji, Y.,Namba, S. Crystal structure of phyllogen, a phyllody-inducing effector protein of phytoplasma. Biochem.Biophys.Res.Commun., 513:952-957, 2019 Cited by PubMed Abstract: Phytoplasmas are plant pathogenic bacteria that often induce unique phyllody symptoms in which the floral organs are transformed into leaf-like structures. Recently, a novel family of bacterial effector genes, called phyllody-inducing genes (phyllogens), was identified as being involved in the induction of phyllody by degrading floral MADS-domain transcription factors (MTFs). However, the structural characteristics of phyllogens are unknown. In this study, we elucidated the crystal structure of PHYL1, a phyllogen of 'Candidatus Phytoplasma asteris' onion yellows strain, at a resolution of 2.4 Å. The structure of PHYL1 consisted of two α-helices connected by a random loop in a coiled-coil manner. In both α-helices, the distributions of hydrophobic residues were conserved among phyllogens. Amino acid insertion mutations into either α-helix resulted in the loss of phyllody-inducing activity and the ability of the phyllogen to degrade floral MTF. In contrast, the same insertion in the loop region did not affect either activity, indicating that both conserved α-helices are important for the function of phyllogens. This is the first report on the crystal structure of an effector protein of phytoplasmas. PubMed: 31010685DOI: 10.1016/j.bbrc.2019.04.060 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.402 Å) |
Structure validation
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