6FPG
Structure of the Ustilago maydis chorismate mutase 1 in complex with a Zea mays kiwellin
Summary for 6FPG
| Entry DOI | 10.2210/pdb6fpg/pdb |
| Descriptor | Chromosome 16, whole genome shotgun sequence, Ripening-related protein 3, CITRIC ACID, ... (4 entities in total) |
| Functional Keywords | smut disease, kiwellin, chorismate, cell invasion |
| Biological source | Ustilago maydis (strain 521 / FGSC 9021) More |
| Total number of polymer chains | 8 |
| Total formula weight | 200099.86 |
| Authors | Altegoer, F.,Steinchen, W.,Bange, G. (deposition date: 2018-02-09, release date: 2019-01-16, Last modification date: 2024-11-06) |
| Primary citation | Han, X.,Altegoer, F.,Steinchen, W.,Binnebesel, L.,Schuhmacher, J.,Glatter, T.,Giammarinaro, P.I.,Djamei, A.,Rensing, S.A.,Reissmann, S.,Kahmann, R.,Bange, G. A kiwellin disarms the metabolic activity of a secreted fungal virulence factor. Nature, 565:650-653, 2019 Cited by PubMed Abstract: Fungi-induced plant diseases affect global food security and plant ecology. The biotrophic fungus Ustilago maydis causes smut disease in maize (Zea mays) plants by secreting numerous virulence effectors that reprogram plant metabolism and immune responses. The secreted fungal chorismate mutase Cmu1 presumably affects biosynthesis of the plant immune signal salicylic acid by channelling chorismate into the phenylpropanoid pathway. Here we show that one of the 20 maize-encoded kiwellins (ZmKWL1) specifically blocks the catalytic activity of Cmu1. ZmKWL1 hinders substrate access to the active site of Cmu1 through intimate interactions involving structural features that are specific to fungal Cmu1 orthologues. Phylogenetic analysis suggests that plant kiwellins have a versatile scaffold that can specifically counteract pathogen effectors such as Cmu1. We reveal the biological activity of a member of the kiwellin family, a widely conserved group of proteins that have previously been recognized only as important human allergens. PubMed: 30651637DOI: 10.1038/s41586-018-0857-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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