6FJL

Structure of IbpS from Dickeya dadantii

Summary for 6FJL

• Entry DOI: 10.2210/pdb6fjl/pdb
• Related: 6HHB
• Descriptor: ABC-type Fe3+ transport system, periplasmic component, ACETATE ION, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: substrate binding protein bacterial effector venus fly-trap, metal binding protein
• Biological source: Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
• Total number of polymer chains: 4
• Total formula weight: 155619.07

Authors

Gueguen-Chaignon, V.,Condemine, G.,Terradot, L. (deposition date: 2018-01-22, release date: 2019-02-06, Last modification date: 2024-05-08)

Primary citation

Liu, L.,Gueguen-Chaignon, V.,Goncalves, I.R.,Rascle, C.,Rigault, M.,Dellagi, A.,Loisel, E.,Poussereau, N.,Rodrigue, A.,Terradot, L.,Condemine, G.
A secreted metal-binding protein protects necrotrophic phytopathogens from reactive oxygen species.
Nat Commun, 10:4853-4853, 2019

PubMed Abstract: 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 HO-induced death. Its 1.7 Å 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.

PubMed: 31649262
DOI: 10.1038/s41467-019-12826-x

Experimental method

X-RAY DIFFRACTION (1.70000035298 Å)