6fjl | pdb_00006fjl

Structure of IbpS from Dickeya dadantii

spinqualitylabelsall models 6fjl, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6fjl is a 4 chain structure with sequence from Dickeya dadantii 3937. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.7000004Å Ligands: ACT, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function E0SCP7_DICD3 Publication Abstract from PubMed Few secreted proteins involved in plant infection common to necrotrophic bacteria, fungi and oomycetes have been identified except for plant cell wall-degrading enzymes. Here we study a family of iron-binding proteins that is present in Gram-negative and Gram-positive bacteria, fungi, oomycetes and some animals. Homolog proteins in the phytopathogenic bacterium Dickeya dadantii (IbpS) and the fungal necrotroph Botrytis cinerea (BcIbp) are involved in plant infection. IbpS is secreted, can bind iron and copper, and protects the bacteria against H2O2-induced death. Its 1.7 A crystal structure reveals a classical Venus Fly trap fold that forms dimers in solution and in the crystal. We propose that secreted Ibp proteins binds exogenous metals and thus limit intracellular metal accumulation and ROS formation in the microorganisms. A secreted metal-binding protein protects necrotrophic phytopathogens from reactive oxygen species.,Liu L, Gueguen-Chaignon V, Goncalves IR, Rascle C, Rigault M, Dellagi A, Loisel E, Poussereau N, Rodrigue A, Terradot L, Condemine G Nat Commun. 2019 Oct 24;10(1):4853. doi: 10.1038/s41467-019-12826-x. PMID:31649262 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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