Crystal structures of EfeB and EfeO in a bacterial siderophore-independent iron transport system
Crystal structures of EfeB and EfeO in a bacterial siderophore-independent iron transport system
复制标题
细菌铁载体依赖性铁转运系统中 EfeB 和 EfeO 的晶体结构
DOI:
10.1016/j.bbrc.2022.01.055
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发表时间:
2022
影响因子:
3.1
通讯作者:
Hashimoto Wataru
中科院分区:
文献类型:
--
作者:
Nakatsuji Sakiko;Okumura Kenji;Takase Ryuichi;Watanabe Daisuke;Mikami Bunzo;Hashimoto Wataru
EfeUOB is a siderophore-independent iron uptake mechanism in bacteria. EfeU, EfeO, and EfeB are a permease, an iron-binding or electron-transfer protein, and a peroxidase, respectively. A Gram-negative bacterium,Sphingomonassp. strain A1, encodes EfeU, EfeO, EfeB together with alginate-binding protein Algp7, a truncated EfeO-like protein (EfeOII), in the genome. The typical EfeO (EfeOI) consists of N-terminal cupredoxin and C-terminal M75 peptidase domains. Here, we detail the structure and function of bacterial EfeB and EfeO. Crystal structures of strain A1 EfeB andEscherichia coliEfeOIwere determined at 2.30 Å and 1.85 Å resolutions, respectively. A molecule of heme involved in oxidase activity was bound to the C-terminal Dyp peroxidase domain of EfeB. Two domains of EfeOIwere connected by a short loop, and a zinc ion was bound to four residues, Glu156, Glu159, Asp173, and Glu255, in the C-terminal M75 peptidase domain. These residues formed tetrahedron geometry suitable for metal binding and are well conserved among various EfeO proteins including Algp7 (EfeOII), although the metal-binding site (HxxE) is proposed in the C-terminal M75 peptidase domain. This is the first report on structure of a typical EfeO with two domains, postulating a novel metal-binding motif “ExxE-//-D-//-E” in the EfeO C-terminal M75 peptidase domain.