6fpg

Structure of the Ustilago maydis chorismate mutase 1 in complex with a Zea mays kiwellinStructure of the Ustilago maydis chorismate mutase 1 in complex with a Zea mays kiwellin

Structural highlights 6fpg is a 8 chain structure with sequence from Ustilago maydis 521 and Zea mays. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CMU1_USTMA Secreted chorismate mutase that is one component of a cocktail of effectors shaping the host metabolome and acting as virulence factors. The enzyme is taken up by plant cells, can spread to neighboring cells where it affects the biosynthesis of the plant immune signal salicylic acid by channelling chorismate into the phenylpropanoid pathway (PubMed:21976020, PubMed:30651637). Interferes with the activity of host cytosolic chorismate mutase CM2 through heterodimerization (PubMed:21976020). Publication Abstract from PubMed 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(1,2). The secreted fungal chorismate mutase Cmu1 presumably affects biosynthesis of the plant immune signal salicylic acid by channelling chorismate into the phenylpropanoid pathway(3). 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. A kiwellin disarms the metabolic activity of a secreted fungal virulence factor.,Han X, Altegoer F, Steinchen W, Binnebesel L, Schuhmacher J, Glatter T, Giammarinaro PI, Djamei A, Rensing SA, Reissmann S, Kahmann R, Bange G Nature. 2019 Jan 16. pii: 10.1038/s41586-018-0857-9. doi:, 10.1038/s41586-018-0857-9. PMID:30651637 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 6fpg, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image