Crystal Structure of a Thioredoxin-like Ferredoxin Encoded Within a Cobalamin Biosynthetic Operon of Rhodobacter capsulatus

IF 1.9 4区 生物学 Q4 BIOCHEMISTRY & MOLECULAR BIOLOGY
Yan-Hao Shen, Wen-Long Cheng, Xiao Wang, Huai-En Dai, Mingzhu Wang, Lin Liu
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引用次数: 0

Abstract

Thioredoxin-like ferredoxin is a small homodimeric protein containing a [2Fe-2S] cluster in each monomer. It is only found in bacteria but its physiological function remains largely unknown. The cobalamin biosynthetic operon in the genome of the purple phototroph Rhodobacter capsulatus encodes a putative ferredoxin dubbed as CfrX. To characterize this protein, we cloned, expressed, purified, and crystalized the recombinant CfrX in the iron-sulfur cluster-bound state, and solved the structure at 2.1-Å resolution. Adopting a typical thioredoxin-like ferredoxin fold, a CfrX monomer binds one [2Fe-2S] cluster through four Cys residues located on two protruding loops. Unexpectedly, CfrX dimerizes in a previously unreported manner. With the structural information, we ascertained CfrX as a thioredoxin-like ferredoxin. While the precise function of CfrX in cobalamin biosynthesis is elusive, a link between CfrX and aerobic cobaltochelatase should exist due to the gene clustering pattern. We also discussed the possible relationship among CfrX, CobW, and CobNST with respect to the [2Fe-2S] cluster.

荚膜红杆菌钴胺素生物合成操纵子编码的类硫氧还蛋白的晶体结构
类硫氧还蛋白是一种小的同型二聚体蛋白,在每个单体中含有一个[2Fe-2S]簇。它只存在于细菌中,但其生理功能在很大程度上仍然未知。紫色光养荚膜红杆菌基因组中的钴胺素生物合成操纵子编码一种假定的铁氧还蛋白,称为CfrX。为了表征该蛋白,我们克隆、表达、纯化和结晶了铁硫簇结合状态的重组CfrX,并以2.1-Å的分辨率对其结构进行了解析。CfrX单体采用典型的类似硫氧还蛋白的铁氧还蛋白折叠,通过位于两个突出环上的四个Cys残基结合一个[2Fe-2S]簇。出乎意料的是,CfrX以一种以前未报道过的方式聚合。根据结构信息,我们确定CfrX是一种类似硫氧还蛋白的铁氧还蛋白。虽然CfrX在钴胺素生物合成中的确切功能尚不清楚,但由于基因聚类模式,CfrX与需氧钴螯合酶之间应该存在联系。我们还讨论了CfrX、CobW和CobNST在[2Fe-2S]簇中的可能关系。
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
The Protein Journal
The Protein Journal 生物-生化与分子生物学
CiteScore
5.20
自引率
0.00%
发文量
57
审稿时长
12 months
期刊介绍: The Protein Journal (formerly the Journal of Protein Chemistry) publishes original research work on all aspects of proteins and peptides. These include studies concerned with covalent or three-dimensional structure determination (X-ray, NMR, cryoEM, EPR/ESR, optical methods, etc.), computational aspects of protein structure and function, protein folding and misfolding, assembly, genetics, evolution, proteomics, molecular biology, protein engineering, protein nanotechnology, protein purification and analysis and peptide synthesis, as well as the elucidation and interpretation of the molecular bases of biological activities of proteins and peptides. We accept original research papers, reviews, mini-reviews, hypotheses, opinion papers, and letters to the editor.
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