2xv1

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

spinqualitylabelsall models 2xv1, resolution 2.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2xv1 is a 1 chain structure with sequence from "vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ECA, FE, PEG, PO4 Related: 2why, 2xuz, 2wi8 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [FEUA_BACSU] Involved in the uptake of iron. Part of the ABC transporter complex FeuABC/YusV involved in import of the catecholate siderophores bacillibactin and enterobactin (Probable). Publication Abstract from PubMed 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 Lambda-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. The siderophore binding protein FeuA shows limited promiscuity toward exogenous triscatecholates.,Peuckert F, Ramos-Vega AL, Miethke M, Schworer CJ, Albrecht AG, Oberthur M, Marahiel MA Chem Biol. 2011 Jul 29;18(7):907-19. PMID:21802011 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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