2XV1

Crystal structure of the triscatecholate siderophore binding protein FeuA from Bacillus subtilis complexed with Ferric MECAM

Summary for 2XV1

• Entry DOI: 10.2210/pdb2xv1/pdb
• Related: 2WHY 2WI8 2XUZ
• Descriptor: IRON-UPTAKE SYSTEM-BINDING PROTEIN, N,N',N''-[BENZENE-1,3,5-TRIYLTRIS(METHYLENE)]TRIS(2,3-DIHYDROXYBENZAMIDE), FE (III) ION, ... (6 entities in total)
• Functional Keywords: transport protein, high affinity iron import, bacillibactin and enterobactin binding, iron transport
• Biological source: BACILLUS SUBTILIS
• Cellular location: Cell membrane; Lipid-anchor (Probable): P40409
• Total number of polymer chains: 1
• Total formula weight: 35778.24

Authors

Peuckert, F.,Miethke, M.,Schwoerer, C.J.,Albrecht, A.G.,Oberthuer, M.,Marahiel, M.A. (deposition date: 2010-10-22, release date: 2011-08-10, Last modification date: 2023-12-20)

Primary citation

Peuckert, F.,Ramos-Vega, A.L.,Miethke, M.,Schwoerer, C.J.,Albrecht, A.G.,Oberthuer, M.,Marahiel, M.A.
The Siderophore Binding Protein Feua Shows Limited Promiscuity Toward Exogenous Triscatecholates
Chem.Biol., 18:907-, 2011

PubMed Abstract: Iron acquisition by siderophores is crucial for survival and virulence of many microorganisms. Here, we investigated the binding of the exogenous siderophore ferric enterobactin and the synthetic siderophore mimic ferric mecam by the triscatecholate binding protein FeuA from Bacillus subtilis at the atomic level. The structural complexes provide molecular insights into the capture mechanism of FeuA for exogenous and synthetic siderophores. The protein-ligand complexes show an exclusive acceptance of Λ-stereoconfigured substrates. Ligand-induced cross-bridging of the complexes was not observed, revealing a different thermodynamic behavior especially of the ferric mecam substrate, which was previously shown to dimerize with the enterobactin binding protein CeuE. The nearly identical overall domain movement of FeuA upon binding of ferric enterobactin or ferric mecam compared with endogenously derived ferric bacillibactin implies the importance of the conserved domain rearrangement for recognition by the transmembrane permease FeuBC, for which the conserved FeuA residues E90 and E221 were proved to be essential.

PubMed: 21802011
DOI: 10.1016/J.CHEMBIOL.2011.05.006

Experimental method

X-RAY DIFFRACTION (2.15 Å)