6qo5

Crystal structure of apo (metal-free) ribonucleotide reductase NrdF from Bacillus anthracis

spinqualitylabelsall models 6qo5, resolution 1.51Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6qo5 is a 2 chain structure with sequence from Bacillus anthracis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.511Å Ligands: CL, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q81TB4_BACAN Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.[PIRNR:PIRNR000355] Publication Abstract from PubMed 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.) 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 A) and in complex with manganese (Mn(II)/Mn(II), 1.30 A). We also report three structures of the protein in complex with iron, either prepared anaerobically (Fe(II)/Fe(II) form, 1.32 A), or prepared aerobically in the photo-reduced Fe(II)/Fe(II) form (1.63 A) and with the partially oxidized metallo-cofactor (1.46 A). 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. 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.,Grave K, Lambert W, Berggren G, Griese JJ, Bennett MD, Logan DT, Hogbom M J Biol Inorg Chem. 2019 Aug 13. pii: 10.1007/s00775-019-01703-z. doi:, 10.1007/s00775-019-01703-z. PMID:31410573 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ribonucleotide reductase 3D structures

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