Sjöberg BM

Activity modulation in anaerobic ribonucleotide reductases: nucleotide binding to the ATP-cone mediates long-range order-disorder transitions in the active site

Bimaï O, Banerjee I, Grinberg IR, ..., Sjöberg BM, Logan DT

- - (-) - [2023-08-16; online 2023-08-16]

Cryo-EM [Service] Structural Proteomics [Service]

A nucleotide-sensing oligomerization mechanism that controls NrdR-dependent transcription of ribonucleotide reductases.

Rozman Grinberg I, Martínez-Carranza M, Bimai O, ..., Sjöberg BM, Stenmark P

Nat Commun 13 (1) 2700 [2022-05-16; online 2022-05-16]

Cryo-EM [Service]

Solution Structure of the dATP-Inactivated Class I Ribonucleotide Reductase From Leeuwenhoekiella blandensis by SAXS and Cryo-Electron Microscopy.

Hasan M, Banerjee I, Rozman Grinberg I, Sjöberg BM, Logan DT

Front Mol Biosci 8 (-) 713608 [2021-07-26; online 2021-07-26]

Cryo-EM [Service]

A ribonucleotide reductase from Clostridium botulinum reveals distinct evolutionary pathways to regulation via the overall activity site.

Martínez-Carranza M, Jonna VR, Lundin D, ..., Stenmark P, Hofer A

J. Biol. Chem. 295 (46) 15576-15587 [2020-11-13; online 2020-09-03]

Bioinformatics Support for Computational Resources [Service] Cryo-EM [Service] Protein Science Facility (PSF) [Service]

Metal-free ribonucleotide reduction powered by a DOPA radical in Mycoplasma pathogens.

Srinivas V, Lebrette H, Lundin D, ..., Sjöberg BM, Högbom M

Nature 563 (7731) 416-420 [2018-11-00; online 2018-10-31]

Global Proteomics and Proteogenomics [Collaborative]