WFRF:(Berggren Gustav)
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- Grāve, KristīneStockholms universitet,Institutionen för biokemi och biofysik,Stockholm Univ, Dept Biochem & Biophys, Svante Arrhenius Vag 16C, S-10691 Stockholm, Sweden (author)
The Bacillus anthracis class Ib ribonucleotide reductase subunit NrdF intrinsically selects manganese over iron
- Article/chapterEnglish2020
Publisher, publication year, extent ...
- 2020-04-15
- Springer Science and Business Media LLC,2020
- printrdacarrier
Numbers
- LIBRIS-ID:oai:DiVA.org:su-181853
- https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-181853URI
- https://doi.org/10.1007/s00775-020-01782-3DOI
- https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-418750URI
Supplementary language notes
- Language:English
- Summary in:English
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Notes
- 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.
Subject headings and genre
- NATURVETENSKAP Biologi hsv//swe
- NATURAL SCIENCES Biological Sciences hsv//eng
- NATURVETENSKAP Kemi hsv//swe
- NATURAL SCIENCES Chemical Sciences hsv//eng
- NATURVETENSKAP Biologi Strukturbiologi hsv//swe
- NATURAL SCIENCES Biological Sciences Structural Biology hsv//eng
- NATURVETENSKAP Biologi Biokemi och molekylärbiologi hsv//swe
- NATURAL SCIENCES Biological Sciences Biochemistry and Molecular Biology hsv//eng
- Metalloprotein
- Metal selectivity
- Quantitative X-ray anomalous dispersion
- Ferritin superfamily
Added entries (persons, corporate bodies, meetings, titles ...)
- Griese, Julia J.Uppsala universitet,Stockholms universitet,Institutionen för biokemi och biofysik,Uppsala University, Sweden,Strukturbiologi,Stockholm Univ, Dept Biochem & Biophys, Svante Arrhenius Vag 16C, S-10691 Stockholm, Sweden(Swepub:uu)julgr393 (author)
- Berggren, GustavUppsala universitet,Molekylär biomimetik(Swepub:uu)guber255 (author)
- Bennett, Matthew D.Stockholms universitet,Institutionen för biokemi och biofysik,Stockholm Univ, Dept Biochem & Biophys, Svante Arrhenius Vag 16C, S-10691 Stockholm, Sweden(Swepub:su)maben (author)
- Högbom, MartinStockholms universitet,Institutionen för biokemi och biofysik,Stockholm Univ, Dept Biochem & Biophys, Svante Arrhenius Vag 16C, S-10691 Stockholm, Sweden(Swepub:su)hogbom (author)
- Stockholms universitetInstitutionen för biokemi och biofysik (creator_code:org_t)
Related titles
- In:Journal of Biological Inorganic Chemistry: Springer Science and Business Media LLC25:4, s. 571-5820949-82571432-1327
Internet link
- https://doi.org/10.1007/s00775-020-01782-3Fulltext
- https://link.springer.com/content/pdf/10.1007/s00775-020-01782-3.pdf
- https://uu.diva-portal.org/smash/get/diva2:1463851/FULLTEXT01.pdffulltext:print
- https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-181853
- https://doi.org/10.1007/s00775-020-01782-3
- https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-418750
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