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The Bacillus anthra...
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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
(författare)
The Bacillus anthracis class Ib ribonucleotide reductase subunit NrdF intrinsically selects manganese over iron
- Artikel/kapitelEngelska2020
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2020-04-15
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Springer Science and Business Media LLC,2020
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printrdacarrier
Nummerbeteckningar
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LIBRIS-ID:oai:DiVA.org:su-181853
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https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-181853URI
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https://doi.org/10.1007/s00775-020-01782-3DOI
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https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-418750URI
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Språk:engelska
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Sammanfattning på:engelska
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Ämneskategori:art swepub-publicationtype
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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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Biuppslag (personer, institutioner, konferenser, titlar ...)
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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
(författare)
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Berggren, GustavUppsala universitet,Molekylär biomimetik(Swepub:uu)guber255
(författare)
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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
(författare)
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Högbom, MartinStockholms universitet,Institutionen för biokemi och biofysik,Stockholm Univ, Dept Biochem & Biophys, Svante Arrhenius Vag 16C, S-10691 Stockholm, Sweden(Swepub:su)hogbom
(författare)
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Stockholms universitetInstitutionen för biokemi och biofysik
(creator_code:org_t)
Sammanhörande titlar
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Ingår i:Journal of Biological Inorganic Chemistry: Springer Science and Business Media LLC25:4, s. 571-5820949-82571432-1327
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