6inr | pdb_00006inr

The crystal structure of phytoplasmal effector causing phyllody symptoms 1 (PHYL1)

spinqualitylabelsall models 6inr, resolution 2.34Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6inr is a 2 chain structure with sequence from 'echinacea purpurea' witches'-broom phytoplasma. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CD Gene: EPWB_v1c1980 ('Echinacea purpurea' witches'-broom phytoplasma) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Phytoplasmas are bacterial plant pathogens which can induce severe symptoms including dwarfism, phyllody and virescence in the infected plant. Because phytoplasmas infect many important crops such as peanut and papaya, they have caused serious agricultural losses. The phytoplasmal effector causing phyllody 1 (PHYL1) is an important pathogenic factor of phytoplasma. PHYL1 affects the biological function of MADS transcription factors by interacting with their K (keratin-like) domain, and thus results in abnormal plant developments such as phyllody. Until now, the lack of PHYL1 structural information has prevented detailed understanding of the binding mechanism between PHYL1 and the MADS transcription factors. Here, we present the crystal structure of PHYL1 from Peanut witches'-broom phytoplasma. PHYL1Pn WB folds into a unique alpha-helical hairpin with exposed hydrophobic residues on its surface that may play an important role in its biological function. Using proteomic approaches, we propose a binding mode of PHYL1Pn WB with the K domain of SEPALLATA3 MADS transcription factor (SEP3_K) and identify the important residues of PHYL1Pn WB for this interaction. Furthermore, by using surface plasmon resonance (SPR), we measure the binding strength of PHYL1Pn WB proteins to SEP3_K. Lastly, based on confocal images, we found that the alpha -Helix 2 of PHYL1Pn WB plays an important role in PHYL1-mediated SEP3 degradation. Taken together, these results provide a structural understanding of the specific binding mechanism between PHYL1Pn WB and SEP3_K. This article is protected by copyright. All rights reserved. Structural insights into the interaction between phytoplasmal effector causing phyllody 1 (PHYL1) and MADS transcription factor.,Liao YT, Lin SS, Lin SJ, Sun WT, Shen BN, Cheng HP, Lin CP, Ko TP, Chen YF, Wang HC Plant J. 2019 Jul 19. doi: 10.1111/tpj.14463. PMID:31323156 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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