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鲍曼不动杆菌菌铁蛋白的晶体结构揭示了菌铁蛋白和铁蛋白亚基的杂多聚体。

The crystal structure of Acinetobacter baumannii bacterioferritin reveals a heteropolymer of bacterioferritin and ferritin subunits.

机构信息

Department of Chemistry, Louisiana State University, Baton Rouge, 70803, USA.

Protein Structure and X-Ray Crystallography Laboratory, University of Kansas, Lawrence, 66047, USA.

出版信息

Sci Rep. 2024 Aug 6;14(1):18242. doi: 10.1038/s41598-024-69156-2.

DOI:10.1038/s41598-024-69156-2
PMID:39107474
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11303784/
Abstract

Iron storage proteins, e.g., vertebrate ferritin, and the ferritin-like bacterioferritin (Bfr) and bacterial ferritin (Ftn), are spherical, hollow proteins that catalyze the oxidation of Fe at binuclear iron ferroxidase centers (FOC) and store the Fe in their interior, thus protecting cells from unwanted Fe/Fe redox cycling and storing iron at concentrations far above the solubility of Fe. Vertebrate ferritins are heteropolymers of H and L subunits with only the H subunits having FOC. Bfr and Ftn were thought to coexist in bacteria as homopolymers, but recent evidence indicates these molecules are heteropolymers assembled from Bfr and Ftn subunits. Despite the heteropolymeric nature of vertebrate and bacterial ferritins, structures have been determined only for recombinant proteins constituted by a single subunit type. Herein we report the structure of Acinetobacter baumannii bacterioferritin, the first structural example of a heteropolymeric ferritin or ferritin-like molecule, assembled from completely overlapping Ftn homodimers harboring FOC and Bfr homodimers devoid of FOC but binding heme. The Ftn homodimers function by catalyzing the oxidation of Fe to Fe, while the Bfr homodimers bind a cognate ferredoxin (Bfd) which reduces the stored Fe by transferring electrons via the heme, enabling Fe mobilization to the cytosol for incorporation in metabolism.

摘要

铁储存蛋白，如脊椎动物铁蛋白和类铁蛋白（Bfr）和细菌铁蛋白（Ftn），是球形的、中空的蛋白质，它们在双核铁亚铁氧化酶中心（FOC）催化 Fe 的氧化，并将 Fe 储存在其内部，从而保护细胞免受不需要的 Fe/Fe 氧化还原循环和储存远远超过 Fe 溶解度的铁。脊椎动物铁蛋白是 H 和 L 亚基的异源聚合物，只有 H 亚基具有 FOC。Bfr 和 Ftn 被认为在细菌中共存，但最近的证据表明这些分子是由 Bfr 和 Ftn 亚基组装而成的同源聚合物。尽管脊椎动物和细菌铁蛋白具有异源聚合性质，但仅确定了由单一亚基类型组成的重组蛋白的结构。在此，我们报告了鲍曼不动杆菌铁蛋白的结构，这是第一个由完全重叠的 Ftn 同源二聚体组成的异源聚合铁蛋白或类铁蛋白分子的结构示例，该二聚体含有 FOC 和 Bfr 同源二聚体，缺乏 FOC，但可结合血红素。Ftn 同源二聚体通过催化 Fe 氧化为 Fe 来发挥作用，而 Bfr 同源二聚体结合同源的铁氧还蛋白（Bfd），通过血红素传递电子还原储存的 Fe，从而使 Fe 动员到细胞质中用于代谢。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f18a/11303784/5c49141c8c02/41598_2024_69156_Fig8_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f18a/11303784/5c788b327439/41598_2024_69156_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f18a/11303784/6fc1c414e96a/41598_2024_69156_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f18a/11303784/955317643146/41598_2024_69156_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f18a/11303784/838cfe1ad6b0/41598_2024_69156_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f18a/11303784/8241575945f1/41598_2024_69156_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f18a/11303784/b0fe594d3ea6/41598_2024_69156_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f18a/11303784/410c176b98cc/41598_2024_69156_Fig7_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f18a/11303784/5c49141c8c02/41598_2024_69156_Fig8_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f18a/11303784/5c788b327439/41598_2024_69156_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f18a/11303784/6fc1c414e96a/41598_2024_69156_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f18a/11303784/955317643146/41598_2024_69156_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f18a/11303784/838cfe1ad6b0/41598_2024_69156_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f18a/11303784/8241575945f1/41598_2024_69156_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f18a/11303784/b0fe594d3ea6/41598_2024_69156_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f18a/11303784/410c176b98cc/41598_2024_69156_Fig7_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f18a/11303784/5c49141c8c02/41598_2024_69156_Fig8_HTML.jpg

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