دورية أكاديمية
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The Bacillus anthracis class Ib ribonucleotide reductase subunit NrdF intrinsically selects manganese over iron.

التفاصيل البيبلوغرافية
العنوان: The Bacillus anthracis class Ib ribonucleotide reductase subunit NrdF intrinsically selects manganese over iron.
المؤلفون: Grāve K; Department of Biochemistry and Biophysics, Stockholm University, Svante Arrhenius väg 16C, 10691, Stockholm, Sweden., Griese JJ; Department of Biochemistry and Biophysics, Stockholm University, Svante Arrhenius väg 16C, 10691, Stockholm, Sweden.; Department of Cell and Molecular Biology, Uppsala University, BMC, Box 596, 75124, Uppsala, Sweden., Berggren G; Department of Chemistry, Ångström Laboratory, Uppsala University, Lägerhyddsvägen 1, 75120, Uppsala, Sweden., Bennett MD; Department of Biochemistry and Biophysics, Stockholm University, Svante Arrhenius väg 16C, 10691, Stockholm, Sweden., Högbom M; Department of Biochemistry and Biophysics, Stockholm University, Svante Arrhenius väg 16C, 10691, Stockholm, Sweden. hogbom@dbb.su.se.
المصدر: Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry [J Biol Inorg Chem] 2020 Jun; Vol. 25 (4), pp. 571-582. Date of Electronic Publication: 2020 Apr 15.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Springer Country of Publication: Germany NLM ID: 9616326 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1432-1327 (Electronic) Linking ISSN: 09498257 NLM ISO Abbreviation: J Biol Inorg Chem Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Berlin : Springer, c1996-
مواضيع طبية MeSH: Bacillus anthracis/*enzymology , Bacterial Proteins/*metabolism , Iron/*metabolism , Manganese/*metabolism , Ribonucleotide Reductases/*metabolism, Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Crystallography, X-Ray ; Iron/chemistry ; Manganese/chemistry ; Models, Molecular ; Protein Conformation ; Ribonucleotide Reductases/chemistry ; Ribonucleotide Reductases/genetics
مستخلص: Correct protein metallation in the complex mixture of the cell is a prerequisite for metalloprotein function. While some metals, such as Cu, are commonly chaperoned, specificity towards metals earlier in the Irving-Williams series is achieved through other means, the determinants of which are poorly understood. The dimetal carboxylate family of proteins provides an intriguing example, as different proteins, while sharing a common fold and the same 4-carboxylate 2-histidine coordination sphere, are known to require either a Fe/Fe, Mn/Fe or Mn/Mn cofactor for function. We previously showed that the R2lox proteins from this family spontaneously assemble the heterodinuclear Mn/Fe cofactor. Here we show that the class Ib ribonucleotide reductase R2 protein from Bacillus anthracis spontaneously assembles a Mn/Mn cofactor in vitro, under both aerobic and anoxic conditions, when the metal-free protein is subjected to incubation with Mn II and Fe II in equal concentrations. This observation provides an example of a protein scaffold intrinsically predisposed to defy the Irving-Williams series and supports the assumption that the Mn/Mn cofactor is the biologically relevant cofactor in vivo. Substitution of a second coordination sphere residue changes the spontaneous metallation of the protein to predominantly form a heterodinuclear Mn/Fe cofactor under aerobic conditions and a Mn/Mn metal center under anoxic conditions. Together, the results describe the intrinsic metal specificity of class Ib RNR and provide insight into control mechanisms for protein metallation.
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فهرسة مساهمة: Keywords: Ferritin superfamily; Metal selectivity; Metalloprotein; Quantitative X-ray anomalous dispersion
المشرفين على المادة: 0 (Bacterial Proteins)
42Z2K6ZL8P (Manganese)
E1UOL152H7 (Iron)
EC 1.17.4.- (NrdF protein, bacteria)
EC 1.17.4.- (Ribonucleotide Reductases)
تواريخ الأحداث: Date Created: 20200417 Date Completed: 20210520 Latest Revision: 20210520
رمز التحديث: 20240829
مُعرف محوري في PubMed: PMC7239806
DOI: 10.1007/s00775-020-01782-3
PMID: 32296998
قاعدة البيانات: MEDLINE
الوصف
تدمد:1432-1327
DOI:10.1007/s00775-020-01782-3