7be8
From Proteopedia
Escherichia coli YtfE (Mn)
Structural highlights
Function[YTFE_ECOLI] Di-iron-containing protein involved in the repair of iron-sulfur clusters damaged by oxidative and nitrosative stress conditions.[1] [2] [3] Publication Abstract from PubMedRepair of Iron Center proteins (RIC) form a family of di-iron proteins that are widely spread in the microbial world. RICs contain a binuclear nonheme iron site in a four-helix bundle fold, two basic features of hemerythrin-like proteins. In this work, we review the data on microbial RICs including how their genes are regulated and contribute to the survival of pathogenic bacteria. We gathered the currently available biochemical, spectroscopic and structural data on RICs with a particular focus on Escherichia coli RIC (also known as YtfE), which remains the best-studied protein with extensive biochemical characterization. Additionally, we present novel structural data for Escherichia coli YtfE harboring a di-manganese site and the protein's affinity for this metal. The networking of protein interactions involving YtfE is also described and integrated into the proposed physiological role as an iron donor for reassembling of stress-damaged iron-sulfur centers. Repair of Iron Center Proteins-A Different Class of Hemerythrin-like Proteins.,Silva LSO, Matias PM, Romao CV, Saraiva LM Molecules. 2022 Jun 23;27(13). pii: molecules27134051. doi:, 10.3390/molecules27134051. PMID:35807291[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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