Structural Basis for Monomer-Dimer Transition of Dri1 Upon Heme Binding.

IF 3.2 4区生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY

Proteins-Structure Function and Bioinformatics Pub Date : 2024-12-13 DOI:10.1002/prot.26778

Xiao-Ying Wang, Jing Zhang, Hong-Yan Li, Chen-Song Dong, Huai-En Dai, Mingzhu Wang, Lin Liu

引用次数: 0

Abstract

Domain related to iron (DRI) contains approximately 90 residues and is involved in iron and heme metabolism. Recent discoveries have annotated Dri1, a DRI-only protein from the cyanobacterium Synechocystis, as a regulator of succinate dehydrogenase in a b-type heme-dependent manner or as a c-type heme oxygenase. Here, we report high-resolution structures of Dri1 in complex with b-type and c-type hemes, respectively. Bis-His-ligated heme is located in the middle of the dimeric Dri1 complex with heme b, as well as in the complex of monomeric Dri1 with c-type heme, but distinct heme binding modes are revealed. Structural analyses suggest that Dri1 may participate in the succinate dehydrogenase activity and/or the metabolism of cytochromes.

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血红素结合时 Dri1 单体-二聚体转变的结构基础

铁相关结构域（DRI）含有约90个残基，参与铁和血红素代谢。最近的研究发现，来自藻胞杆菌的dr1蛋白作为琥珀酸脱氢酶的b型血红素依赖方式或c型血红素加氧酶的调节因子。在这里，我们分别报道了Dri1与b型血红素和c型血红素复合物的高分辨率结构。双his连接血红素位于二聚体Dri1与血红素b复合物的中间，以及单体Dri1与c型血红素复合物的中间，但显示出不同的血红素结合模式。结构分析表明，Dri1可能参与琥珀酸脱氢酶活性和/或细胞色素的代谢。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Proteins-Structure Function and Bioinformatics 生物-生化与分子生物学

CiteScore

5.90

自引率

3.40%

发文量

172

审稿时长

3 months

期刊介绍： PROTEINS : Structure, Function, and Bioinformatics publishes original reports of significant experimental and analytic research in all areas of protein research: structure, function, computation, genetics, and design. The journal encourages reports that present new experimental or computational approaches for interpreting and understanding data from biophysical chemistry, structural studies of proteins and macromolecular assemblies, alterations of protein structure and function engineered through techniques of molecular biology and genetics, functional analyses under physiologic conditions, as well as the interactions of proteins with receptors, nucleic acids, or other specific ligands or substrates. Research in protein and peptide biochemistry directed toward synthesizing or characterizing molecules that simulate aspects of the activity of proteins, or that act as inhibitors of protein function, is also within the scope of PROTEINS. In addition to full-length reports, short communications (usually not more than 4 printed pages) and prediction reports are welcome. Reviews are typically by invitation; authors are encouraged to submit proposed topics for consideration.