2XV1

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

2XV1 の概要

• エントリーDOI: 10.2210/pdb2xv1/pdb
• 関連するPDBエントリー: 2WHY 2WI8 2XUZ
• 分子名称: 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)
• 機能のキーワード: transport protein, high affinity iron import, bacillibactin and enterobactin binding, iron transport
• 由来する生物種: BACILLUS SUBTILIS
• 細胞内の位置: Cell membrane; Lipid-anchor (Probable): P40409
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35778.24

構造登録者

Peuckert, F.,Miethke, M.,Schwoerer, C.J.,Albrecht, A.G.,Oberthuer, M.,Marahiel, M.A. (登録日: 2010-10-22, 公開日: 2011-08-10, 最終更新日: 2023-12-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.15 Å)