Structural insights into a novel family of integral membrane siderophore reductases
Structural insights into a novel family of integral membrane siderophore reductases
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DOI：
10.1073/pnas.2101952118
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发表时间：
2021-08-24
影响因子：
11.1
通讯作者：
Tidow, Henning
中科院分区：
文献类型：
--
作者：
Josts, Inokentijs;Veith, Katharina;Tidow, Henning
革兰氏阴性细菌使用 TonB 依赖性转运蛋白通过其外膜吸收必需离子 Fe3+ 作为铁铁载体复合物。然而，随后穿过内膜的途径因许多细菌种类和铁载体化学性质而异，并且尚不清楚。在这里，我们报道了参与铁铁载体吸收的内膜蛋白 FoxB（来自铜绿假单胞菌）的晶体结构。该结构揭示了两个紧密结合的血红素分子的折叠。结合体外还原测定和体内铁摄取研究，这些结果确定 FoxB 是一种内膜还原酶，参与 Fesiderophore 摄取过程中从铁胺中释放铁。
Gram-negative bacteria take up the essential ion Fe3+ as ferricsiderophore complexes through their outer membrane using TonBdependent transporters. However, the subsequent route through the inner membrane differs across many bacterial species and siderophore chemistries and is not understood in detail. Here, we report the crystal structure of the inner membrane protein FoxB (from Pseudomonas aeruginosa) that is involved in Fe-siderophore uptake. The structure revealed a fold with two tightly bound heme molecules. In combination with in vitro reduction assays and in vivo iron uptake studies, these results establish FoxB as an inner membrane reductase involved in the release of iron from ferrioxamine during Fesiderophore uptake.