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Redox-induced struc...
Redox-induced structural changes in the di-iron and di-manganese forms of Bacillus anthracis ribonucleotide reductase subunit NrdF suggest a mechanism for gating of radical access
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- Grāve, Kristīne (författare)
- Stockholms universitet,Institutionen för biokemi och biofysik,Stockholm University
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- Lambert, Wietske (författare)
- PRA Health Sciences, Assen, The Netherlands
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- Berggren, Gustav (författare)
- Uppsala University,Uppsala universitet,Molekylär biomimetik
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- Griese, Julia J. (författare)
- Stockholm University,Uppsala universitet,Stockholms universitet,Institutionen för biokemi och biofysik,Uppsala University, Sweden,Strukturbiologi,Department of Biochemistry and Biophysics, Stockholm University
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- Bennett, Matthew D. (författare)
- Stockholms universitet,Institutionen för biokemi och biofysik,Stockholm University
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- Logan, Derek T. (författare)
- Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
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- Högbom, Martin (författare)
- Stockholms universitet,Institutionen för biokemi och biofysik,Stockholm University
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(creator_code:org_t)
- 2019-08-13
- 2019
- Engelska.
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Ingår i: Journal of Biological Inorganic Chemistry. - : Springer Science and Business Media LLC. - 0949-8257 .- 1432-1327. ; 24:6, s. 849-861
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Abstract
Ämnesord
Stäng
- Class Ib ribonucleotide reductases (RNR) utilize a di-nuclear manganese or iron cofactor for reduction of superoxide or molecular oxygen, respectively. This generates a stable tyrosyl radical (Y center dot) in the R2 subunit (NrdF), which is further used for ribonucleotide reduction in the R1 subunit of RNR. Here, we report high-resolution crystal structures of Bacillus anthracis NrdF in the metal-free form (1.51 angstrom) and in complex with manganese (Mn-II/Mn-II, 1.30 angstrom). We also report three structures of the protein in complex with iron, either prepared anaerobically (Fe-II/Fe-II form, 1.32 angstrom), or prepared aerobically in the photo-reduced Fe-II/Fe-II form (1.63 angstrom) and with the partially oxidized metallo-cofactor (1.46 angstrom). The structures reveal significant conformational dynamics, likely to be associated with the generation, stabilization, and transfer of the radical to the R1 subunit. Based on observed redox-dependent structural changes, we propose that the passage for the superoxide, linking the FMN cofactor of NrdI and the metal site in NrdF, is closed upon metal oxidation, blocking access to the metal and radical sites. In addition, we describe the structural mechanics likely to be involved in this process.
Ämnesord
- 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)
Nyckelord
- Oxidoreductase
- Metalloprotein
- Carboxylate shift
- X-ray crystallography
- Ferritin superfamily
- Biochemistry
- biokemi
- Carboxylate shift
- Ferritin superfamily
- Metalloprotein
- Oxidoreductase
- X-ray crystallography
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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