8J4J

X-ray structure of a ferric ion-binding protein A (FbpA) from Vibrio metschnikovii in complex with ferric ion

8J4J の概要

• エントリーDOI: 10.2210/pdb8j4j/pdb
• 分子名称: Ferric iron ABC transporter iron-binding protein, FE (III) ION, CARBONATE ION, ... (4 entities in total)
• 機能のキーワード: ferric binding protein, fbpa, danshensu, vibrio metschnikovii, metal binding protein
• 由来する生物種: Vibrio metschnikovii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33676.62

構造登録者

Lu, P.,Jiang, J.,Nagata, K. (登録日: 2023-04-20, 公開日: 2024-01-10, 最終更新日: 2024-02-07)

主引用文献

Lu, P.,Jiang, J.,Liu, C.,Okuda, S.,Itoh, H.,Okamoto, K.,Suzuki, M.,Nagata, K.
Molecular mechanism of Fe 3+ binding inhibition to Vibrio metschnikovii ferric ion-binding protein, FbpA, by rosmarinic acid and its hydrolysate, danshensu.
Protein Sci., 33:e4881-e4881, 2024

PubMed Abstract: Global warming has increased the growth of pathogenic Vibrio bacteria, which can cause foodborne illnesses and death. Vibrio bacteria require iron for growth and survival. They utilize a ferric ion-binding protein (FbpA) to bind and transport Fe into the cell. FbpA from Vibrio metschnikovii (Vm) is a potential target for inhibiting its growth. Rosmarinic acid (RA) can block the binding of VmFbpA to Fe ; however, the molecular mechanism of Fe binding and RA inhibition to VmFbpA is unclear. In this study, we used x-ray crystallography to determine the Fe -binding mode of VmFbpA and the mechanism of RA inhibition. The structures revealed that in the Fe bound form, Fe was coordinated to VmFbpA by two Tyr residues, two HCO ions, and two water molecules in a six-coordinated geometry. In contrast, in the inhibitor bound form, RA was initially bound to VmFbpA following gel filtration purification, but it was hydrolyzed to danshensu (DSS), which occupied the binding site as shown in an electron density map and reverse phase chromatography (RPC) analysis. Both RA and DSS exhibited a stronger binding affinity to VmFbpA, higher Fe reduction capacity, and more potent bacteriostatic effect on V. metschnikovii compared with caffeic acid (CA), another hydrolysis product of RA. These results provide insight into the mechanism of iron acquisition by V. metschnikovii and inhibition by RA and DSS. Our findings offer clues on the development of effective strategies to prevent Vibrio infections.

PubMed: 38143427
DOI: 10.1002/pro.4881

実験手法

X-RAY DIFFRACTION (2.15 Å)